Cry2

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust shows substantially faster clustering and de-clustering kinetics than Cry2.

This variant-called BcLOVclust-clustered over many cycles with substantially faster clustering and de-clustering kinetics compared to the widely used optogenetic clustering protein Cry2.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is an engineered BcLOV4-derived variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

Herein we identify key amino acids that couple BcLOV4 clustering to membrane binding, allowing us to engineer a variant that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust is temperature sensitive, and its light-induced clusters dissolve faster at higher temperature despite constant illumination.

Like wt BcLOV4, BcLOVclust activity was sensitive to temperature: light-induced clusters spontaneously dissolved at a rate that increased with temperature despite constant illumination.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be strengthened by appending a FUS intrinsically disordered region or by selecting the fused fluorescent protein.

The magnitude of clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by selecting the appropriate fluorescent protein to which it was fused.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to control independent protein condensates with light.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

BcLOVclust is currently best suited for cells and organisms cultured below approximately 30 °C rather than physiological mammalian temperatures.

While its usage is currently best suited in cells and organisms that can be cultured below ∼30 °C, a deeper understanding of BcLOVclust thermal response will further enable its use at physiological mammalian temperatures.

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

Current use of BcLOVclust is suited for organisms that can be cultured below approximately 30 degrees Celsius.

While its usage is currently suited for organisms that can be cultured below ∼30 °C

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

BcLOVclust can be used to control signaling proteins and stress granules in mammalian cells.

BcLOVclust could also be applied to control signaling proteins and stress granules in mammalian cells.

LAB maps E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

We show that LAB can map E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

LAB maps E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

We show that LAB can map E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

LAB maps E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

We show that LAB can map E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

LAB maps E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

We show that LAB can map E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

LAB maps E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

We show that LAB can map E-cadherin-binding partners with higher accuracy and significantly fewer false positives than TurboID.

CRY2 is essential in regulating skeletal muscle repair.

Therefore, CRY2 is essential in regulating skeletal muscle repair.

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

BcLOVclust has dramatically faster clustering and de-clustering kinetics than Cry2.

BcLOVclust, clustered over many cycles with dramatically faster clustering and de-clustering kinetics compared to Cry2

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

LAB fuses the two halves of split-TurboID to the photodimeric proteins CRY2 and CIB1.

Our technology, called light-activated BioID (LAB), fuses the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

Wild-type CRY2 and the CRY2 variant are degraded by a lysosomal-mediated degradation pathway.

Further studies revealed that wild-type and CRY2 variants are degraded by the lysosomal-mediated degradation pathway, a mechanism not previously associated with CRY2.

Wild-type CRY2 and the CRY2 variant are degraded by a lysosomal-mediated degradation pathway.

Further studies revealed that wild-type and CRY2 variants are degraded by the lysosomal-mediated degradation pathway, a mechanism not previously associated with CRY2.

Wild-type CRY2 and the CRY2 variant are degraded by a lysosomal-mediated degradation pathway.

Further studies revealed that wild-type and CRY2 variants are degraded by the lysosomal-mediated degradation pathway, a mechanism not previously associated with CRY2.

Wild-type CRY2 and the CRY2 variant are degraded by a lysosomal-mediated degradation pathway.

Further studies revealed that wild-type and CRY2 variants are degraded by the lysosomal-mediated degradation pathway, a mechanism not previously associated with CRY2.

Wild-type CRY2 and the CRY2 variant are degraded by a lysosomal-mediated degradation pathway.

Further studies revealed that wild-type and CRY2 variants are degraded by the lysosomal-mediated degradation pathway, a mechanism not previously associated with CRY2.

Wild-type CRY2 and the CRY2 variant are degraded by a lysosomal-mediated degradation pathway.

Further studies revealed that wild-type and CRY2 variants are degraded by the lysosomal-mediated degradation pathway, a mechanism not previously associated with CRY2.

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

A BcLOV4 variant was engineered that clusters in the cytoplasm and does not associate with the membrane in response to blue light.

allowing us to engineer a variant of BcLOV4 that clusters in the cytoplasm and does not associate with the membrane in response to blue light

Loss of CRY2 increases the number of PAX7-positive cells associated with myotubes, suggesting increased reserve cell production.

Immunostaining revealed that the number of mononucleated paired box protein 7 (PAX7+) cells associated with myotubes formed by CRY2-/- cells was increased compared with CRY2+/+ cells, suggesting that more reserve cells were produced in the absence of CRY2.

Arabidopsis cryptochrome 2 is employed for optogenetic induction of caspase-8-mediated apoptosis.

CRY2-deficient myoblasts survive better in ischemic muscle.

CRY2 deficient myoblasts survived better in ischemic muscle.

Deletion of CRY2 enhances muscle regeneration.

Using the skeletal muscle lineage and satellite cell-specific CRY2 knockout mice (CRY2scko), we show that the deletion of CRY2 enhances muscle regeneration.

Deletion of CRY2 stimulates myoblast proliferation.

Single myofiber analysis revealed that deletion of CRY2 stimulates the proliferation of myoblasts.

Loss of CRY2 enhances myoblast differentiation, evidenced by increased MyHC expression and myotube formation.

The differentiation potential of myoblasts was enhanced by the loss of CRY2 evidenced by increased expression of myosin heavy chain (MyHC) and myotube formation in CRY2-/- cells versus CRY2+/+ cells.

Loss of CRY2 activates ERK1/2 signaling and ETS1, and ETS1 binds the PAX7 promoter to induce PAX7 transcription.

Loss of CRY2 leads to the activation of the ERK1/2 signaling pathway and ETS1, which binds to the promoter of PAX7 to induce its transcription.

Ser-420 of CRY2 is required for interaction with the E3 ligases FBXL3 and FBXL21.

which suggests Ser-420 of CRY2 is required for the interaction with E3 ligases

Ser-420 of CRY2 is required for interaction with the E3 ligases FBXL3 and FBXL21.

which suggests Ser-420 of CRY2 is required for the interaction with E3 ligases

Ser-420 of CRY2 is required for interaction with the E3 ligases FBXL3 and FBXL21.

which suggests Ser-420 of CRY2 is required for the interaction with E3 ligases

Ser-420 of CRY2 is required for interaction with the E3 ligases FBXL3 and FBXL21.

which suggests Ser-420 of CRY2 is required for the interaction with E3 ligases

Ser-420 of CRY2 is required for interaction with the E3 ligases FBXL3 and FBXL21.

which suggests Ser-420 of CRY2 is required for the interaction with E3 ligases

Ser-420 of CRY2 is required for interaction with the E3 ligases FBXL3 and FBXL21.

which suggests Ser-420 of CRY2 is required for the interaction with E3 ligases

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

Upon blue light illumination, CRY2 and CIB1 dimerize, reconstitute split-TurboID, and initiate biotinylation.

upon illumination with blue light, CRY2 and CIB1 dimerize, reconstitute split-TurboID and initiate biotinylation

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

BcLOVclust clustering magnitude can be increased by appending a FUS intrinsically disordered region or by optimizing the fused fluorescent protein.

The magnitude of BcLOVclust clustering could be strengthened by appending an intrinsically disordered region from the fused in sarcoma (FUS) protein, or by optimizing the fluorescent protein to which it was fused.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

At low temperatures, BcLOVclust and Cry2 can be multiplexed in the same cells to independently control protein condensates.

At low temperatures, BcLOVclust and Cry2 could be multiplexed in the same cells, allowing light control of independent protein condensates.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

Turning off the light causes CRY2 and CIB1 to dissociate and halts biotinylation.

Turning off the light leads to the dissociation of CRY2 and CIB1 and halts biotinylation.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

BcLOVclust retains temperature sensitivity such that light-induced clustering is transient and spontaneous declustering increases with temperature.

BcLOVclust retained the temperature sensitivity of BcLOV4 such that light induced clustering was transient, and the rate of spontaneous declustering increased with temperature.

Light-activated BioID is a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

Here, we present a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

Light-activated BioID is a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

Here, we present a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

Light-activated BioID is a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

Here, we present a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

Light-activated BioID is a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

Here, we present a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

Light-activated BioID is a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

Here, we present a light-activated proximity labeling technology for mapping protein-protein interactions at the cell membrane with high accuracy and precision.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.

We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.

We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC was benchmarked in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

We benchmark this tool, optoSynC, in Caenorhabditis elegans, zebrafish, and murine hippocampal neurons.

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

optoSynC is a highly efficient non-ionic optogenetic silencer.

optoSynC is a highly efficient, ‘non-ionic’ optogenetic silencer

LAB is generated by fusing split-TurboID halves to the photodimeric proteins CRY2 and CIB1.

Our system, called Light Activated BioID (LAB), is generated by fusing the two halves of the split-TurboID proximity labeling enzyme to the photodimeric proteins CRY2 and CIB1.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

optoSynC can inhibit exocytosis for several hours at very low light intensities.

optoSynC can inhibit exocytosis for several hours, at very low light intensities

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Arabidopsis cryptochromes are blue light photoreceptors that regulate plant growth, development, and metabolism.

Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants.

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

Both the N-terminal and C-terminal domains of Arabidopsis cryptochromes participate in light-induced interactions with multiple signaling proteins including the COP1/SPA E3 ubiquitin ligase.

Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase...

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

optoSynC-induced locomotion silencing occurs with tau_on of about 7.2 seconds and recovery after light-off with tau_off of about 6.5 minutes.

Locomotion silencing occurs with tauon ~7.2 s and recovers with tauoff ~6.5 min after light-off.

Blue light exposure causes CRY2 and CIB1 to dimerize, reconstitute split-TurboID, and biotinylate proximate proteins in the LAB system.

upon exposure to blue light, CRY2 and CIB1 dimerize, reconstitute the split-TurboID enzyme, and biotinylate proximate proteins

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

optoSynC uses light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission by clustering synaptic vesicles.

Here, we use light-evoked homo-oligomerization of cryptochrome CRY2 to silence synaptic transmission, by clustering synaptic vesicles (SVs).

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Upon blue light exposure, inactive monomeric Arabidopsis cryptochromes undergo phosphorylation and oligomerization that are crucial to cryptochrome function.

Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.

We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

Arabidopsis cryptochrome signaling involves interactions with transcription factors, hormone signaling intermediates, chromatin-remodeling proteins, and proteins involved in RNA N6 adenosine methylation.

These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC can inhibit exocytosis for several hours at very low light intensities.

Further, optoSynC can inhibit exocytosis for several hours, at very low light intensities.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC causes rapid locomotion silencing with an activation time constant of approximately 15 seconds and recovery after light-off with a time constant of approximately 10 minutes.

Locomotion silencing is rapid (tau on ∼15 s) and recovers quickly (tau off ∼10 min) after light-off.

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s

optoSynC clusters synaptic vesicles within 25 seconds.

optoSynC clusters SVs within 25 s