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 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 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.

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.

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.

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.

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

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.

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

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.

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.

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.

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.

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 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

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...

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 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.

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.

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 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 does not affect ion currents, biochemistry, or synaptic proteins.

does not affect ion currents, biochemistry or synaptic proteins

optoSynC does not affect ion currents, biochemistry, or synaptic proteins.

does not affect ion currents, biochemistry or synaptic proteins

optoSynC does not affect ion currents, biochemistry, or synaptic proteins.

does not affect ion currents, biochemistry or synaptic proteins

optoSynC does not affect ion currents, biochemistry, or synaptic proteins.

does not affect ion currents, biochemistry or synaptic proteins

optoSynC does not affect ion currents, biochemistry, or synaptic proteins.

does not affect ion currents, biochemistry or synaptic proteins

optoSynC does not affect ion currents, biochemistry, or synaptic proteins.

does not affect ion currents, biochemistry or synaptic proteins

optoSynC does not affect ion currents, biochemistry, or synaptic proteins.

does not affect ion currents, biochemistry or synaptic proteins

optoSynC clusters synaptic vesicles, observable by electron microscopy.

optoSynC clusters SVs, observable by electron microscopy.

optoSynC clusters synaptic vesicles, observable by electron microscopy.

optoSynC clusters SVs, observable by electron microscopy.

optoSynC clusters synaptic vesicles, observable by electron microscopy.

optoSynC clusters SVs, observable by electron microscopy.

optoSynC clusters synaptic vesicles, observable by electron microscopy.

optoSynC clusters SVs, observable by electron microscopy.

optoSynC clusters synaptic vesicles, observable by electron microscopy.

optoSynC clusters SVs, observable by electron microscopy.

optoSynC clusters synaptic vesicles, observable by electron microscopy.

optoSynC clusters SVs, observable by electron microscopy.

optoSynC clusters synaptic vesicles, observable by electron microscopy.

optoSynC clusters SVs, observable by electron microscopy.

The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

CRY2-mediated blue-light signaling enhances freezing tolerance.

CRY2-mediated blue-light signaling enhances freezing tolerance

CRY2-mediated blue-light signaling enhances freezing tolerance.

CRY2-mediated blue-light signaling enhances freezing tolerance

CRY2-mediated blue-light signaling enhances freezing tolerance.

CRY2-mediated blue-light signaling enhances freezing tolerance

CRY2-mediated blue-light signaling enhances freezing tolerance.

CRY2-mediated blue-light signaling enhances freezing tolerance

CRY2-mediated blue-light signaling enhances freezing tolerance.

CRY2-mediated blue-light signaling enhances freezing tolerance

CRY2-mediated blue-light signaling enhances freezing tolerance.

CRY2-mediated blue-light signaling enhances freezing tolerance

CRY2-mediated blue-light signaling enhances freezing tolerance.

CRY2-mediated blue-light signaling enhances freezing tolerance

Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate distinct structural elements and critical residues that dynamically participate in photo-induced oligomerization.

Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate distinct structural elements and critical residues that dynamically partake in photo-induced oligomerization.

The study offers an updated model of cryptochrome photoactivation mechanism and its regulation by interacting proteins.

Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.

Cold-stabilized CRY2 competes with HY5 and attenuates the HY5-COP1 interaction, allowing HY5 to accumulate at cold temperatures.

cold-stabilized CRY2 competes with the transcription factor HY5 to attenuate the HY5-COP1 interaction, thereby allowing HY5 to accumulate at cold temperatures

Cold-stabilized CRY2 competes with HY5 and attenuates the HY5-COP1 interaction, allowing HY5 to accumulate at cold temperatures.

cold-stabilized CRY2 competes with the transcription factor HY5 to attenuate the HY5-COP1 interaction, thereby allowing HY5 to accumulate at cold temperatures

Cold-stabilized CRY2 competes with HY5 and attenuates the HY5-COP1 interaction, allowing HY5 to accumulate at cold temperatures.

cold-stabilized CRY2 competes with the transcription factor HY5 to attenuate the HY5-COP1 interaction, thereby allowing HY5 to accumulate at cold temperatures

Cold-stabilized CRY2 competes with HY5 and attenuates the HY5-COP1 interaction, allowing HY5 to accumulate at cold temperatures.

cold-stabilized CRY2 competes with the transcription factor HY5 to attenuate the HY5-COP1 interaction, thereby allowing HY5 to accumulate at cold temperatures

Cold-stabilized CRY2 competes with HY5 and attenuates the HY5-COP1 interaction, allowing HY5 to accumulate at cold temperatures.

cold-stabilized CRY2 competes with the transcription factor HY5 to attenuate the HY5-COP1 interaction, thereby allowing HY5 to accumulate at cold temperatures

Cold-stabilized CRY2 competes with HY5 and attenuates the HY5-COP1 interaction, allowing HY5 to accumulate at cold temperatures.

cold-stabilized CRY2 competes with the transcription factor HY5 to attenuate the HY5-COP1 interaction, thereby allowing HY5 to accumulate at cold temperatures

Cold-stabilized CRY2 competes with HY5 and attenuates the HY5-COP1 interaction, allowing HY5 to accumulate at cold temperatures.

cold-stabilized CRY2 competes with the transcription factor HY5 to attenuate the HY5-COP1 interaction, thereby allowing HY5 to accumulate at cold temperatures

The CRY2-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana.

we demonstrate that the CRYPTOCHROME2 (CRY2)-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana

The CRY2-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana.

we demonstrate that the CRYPTOCHROME2 (CRY2)-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana

The CRY2-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana.

we demonstrate that the CRYPTOCHROME2 (CRY2)-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana

The CRY2-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana.

we demonstrate that the CRYPTOCHROME2 (CRY2)-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana

The CRY2-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana.

we demonstrate that the CRYPTOCHROME2 (CRY2)-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana

The CRY2-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana.

we demonstrate that the CRYPTOCHROME2 (CRY2)-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana

The CRY2-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana.

we demonstrate that the CRYPTOCHROME2 (CRY2)-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis thaliana

Blue light-induced phosphorylated forms of CRY2 are stabilized by cold stress.

phosphorylated forms of CRY2 induced by blue light are stabilized by cold stress

Blue light-induced phosphorylated forms of CRY2 are stabilized by cold stress.

phosphorylated forms of CRY2 induced by blue light are stabilized by cold stress

Blue light-induced phosphorylated forms of CRY2 are stabilized by cold stress.

phosphorylated forms of CRY2 induced by blue light are stabilized by cold stress

Blue light-induced phosphorylated forms of CRY2 are stabilized by cold stress.

phosphorylated forms of CRY2 induced by blue light are stabilized by cold stress

Blue light-induced phosphorylated forms of CRY2 are stabilized by cold stress.

phosphorylated forms of CRY2 induced by blue light are stabilized by cold stress

Blue light-induced phosphorylated forms of CRY2 are stabilized by cold stress.

phosphorylated forms of CRY2 induced by blue light are stabilized by cold stress

Blue light-induced phosphorylated forms of CRY2 are stabilized by cold stress.

phosphorylated forms of CRY2 induced by blue light are stabilized by cold stress

The study determined the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.

In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.

Cryptochrome 2 and a light-activated degron are used for optogenetic control of gene expression.

Optogenetic Control of Gene Expression Using Cryptochrome 2 and a Light-Activated Degron

Cryptochromes are blue-light receptors that mediate photoresponses in plants.

Cryptochromes are blue-light receptors that mediate photoresponses in plants.

Cryptochromes integrate blue-light signals with other internal and external signals to optimize plant growth and development.

These two mechanisms enable cryptochromes to integrate blue-light signals with other internal and external signals to optimize plant growth and development.

Cryptochrome homooligomerization alters the affinity of cryptochromes for cryptochrome-interacting proteins to form various cryptochrome complexes.

which alters the affinity of cryptochromes interacting with cryptochrome-interacting proteins to form various cryptochrome complexes

In darkness cryptochromes are physiologically inactive monomers, and photon absorption leads to conformational change and cryptochrome homooligomerization.

Cryptochromes exist as physiologically inactive monomers in the dark; the absorption of photons leads to conformational change and cryptochrome homooligomerization

Photoresponsive protein-protein interaction is the primary mode of signal transduction of cryptochromes.

Photoresponsive protein-protein interaction is the primary mode of signal transduction of cryptochromes.

Cryptochrome activity is regulated by photooligomerization, dark monomerization, cryptochrome regulatory proteins, and cryptochrome phosphorylation, ubiquitination, and degradation.

The activity of cryptochromes is regulated by photooligomerization; dark monomerization; cryptochrome regulatory proteins; and cryptochrome phosphorylation, ubiquitination, and degradation.

Among the compared strategies, the CRY2-integrated approach that combines light-induced membrane recruitment and iTrkB homo-interaction was the most efficient at activating TrkB receptors.

By comparing all the different strategies, we find that the CRY2-integrated approach to achieve light-induced cell membrane recruitment and homo-interaction of iTrkB is most efficient in activating TrkB receptors.

Among the compared strategies, the CRY2-integrated approach that combines light-induced membrane recruitment and iTrkB homo-interaction was the most efficient at activating TrkB receptors.

By comparing all the different strategies, we find that the CRY2-integrated approach to achieve light-induced cell membrane recruitment and homo-interaction of iTrkB is most efficient in activating TrkB receptors.

Among the compared strategies, the CRY2-integrated approach that combines light-induced membrane recruitment and iTrkB homo-interaction was the most efficient at activating TrkB receptors.

By comparing all the different strategies, we find that the CRY2-integrated approach to achieve light-induced cell membrane recruitment and homo-interaction of iTrkB is most efficient in activating TrkB receptors.

Among the compared strategies, the CRY2-integrated approach that combines light-induced membrane recruitment and iTrkB homo-interaction was the most efficient at activating TrkB receptors.

By comparing all the different strategies, we find that the CRY2-integrated approach to achieve light-induced cell membrane recruitment and homo-interaction of iTrkB is most efficient in activating TrkB receptors.

Among the compared strategies, the CRY2-integrated approach that combines light-induced membrane recruitment and iTrkB homo-interaction was the most efficient at activating TrkB receptors.

By comparing all the different strategies, we find that the CRY2-integrated approach to achieve light-induced cell membrane recruitment and homo-interaction of iTrkB is most efficient in activating TrkB receptors.

Among the compared strategies, the CRY2-integrated approach that combines light-induced membrane recruitment and iTrkB homo-interaction was the most efficient at activating TrkB receptors.

By comparing all the different strategies, we find that the CRY2-integrated approach to achieve light-induced cell membrane recruitment and homo-interaction of iTrkB is most efficient in activating TrkB receptors.

Among the compared strategies, the CRY2-integrated approach that combines light-induced membrane recruitment and iTrkB homo-interaction was the most efficient at activating TrkB receptors.

By comparing all the different strategies, we find that the CRY2-integrated approach to achieve light-induced cell membrane recruitment and homo-interaction of iTrkB is most efficient in activating TrkB receptors.

BEE1 promotes flowering in a CRY2 partially dependent manner.

BEE1 promotes flowering in a blue light photoreceptor CRYPTOCHROME 2 (CRY2) partially dependent manner

The optical TrkB activation strategy is generalizable to other optical homo-dimerizers, including an aureochrome 1 LOV-domain-based implementation.

we prove that such strategies are generalizable to other optical homo-dimerizers by demonstrating the optical TrkB activation based on the light-oxygen-voltage domain of aureochrome 1 from Vaucheria frigida

The optical TrkB activation strategy is generalizable to other optical homo-dimerizers, including an aureochrome 1 LOV-domain-based implementation.

we prove that such strategies are generalizable to other optical homo-dimerizers by demonstrating the optical TrkB activation based on the light-oxygen-voltage domain of aureochrome 1 from Vaucheria frigida

The optical TrkB activation strategy is generalizable to other optical homo-dimerizers, including an aureochrome 1 LOV-domain-based implementation.

we prove that such strategies are generalizable to other optical homo-dimerizers by demonstrating the optical TrkB activation based on the light-oxygen-voltage domain of aureochrome 1 from Vaucheria frigida

The optical TrkB activation strategy is generalizable to other optical homo-dimerizers, including an aureochrome 1 LOV-domain-based implementation.

we prove that such strategies are generalizable to other optical homo-dimerizers by demonstrating the optical TrkB activation based on the light-oxygen-voltage domain of aureochrome 1 from Vaucheria frigida

The optical TrkB activation strategy is generalizable to other optical homo-dimerizers, including an aureochrome 1 LOV-domain-based implementation.

we prove that such strategies are generalizable to other optical homo-dimerizers by demonstrating the optical TrkB activation based on the light-oxygen-voltage domain of aureochrome 1 from Vaucheria frigida

The optical TrkB activation strategy is generalizable to other optical homo-dimerizers, including an aureochrome 1 LOV-domain-based implementation.

we prove that such strategies are generalizable to other optical homo-dimerizers by demonstrating the optical TrkB activation based on the light-oxygen-voltage domain of aureochrome 1 from Vaucheria frigida

The optical TrkB activation strategy is generalizable to other optical homo-dimerizers, including an aureochrome 1 LOV-domain-based implementation.

we prove that such strategies are generalizable to other optical homo-dimerizers by demonstrating the optical TrkB activation based on the light-oxygen-voltage domain of aureochrome 1 from Vaucheria frigida

Activity of a split synthetic zinc-finger transcription factor is reconstituted using CRY2- and CIB1-mediated light-induced dimerization.

We reconstitute activity of a split synthetic zinc-finger transcription factor (TF) using light-induced dimerization mediated by the proteins CRY2 and CIB1.

BEE1 integrates BES1 and CRY2 in mediating flowering, and BES1-BEE1-FT is a signaling pathway regulating photoperiodic flowering.

Our findings indicate that BEE1 is the integrator of BES1 and CRY2 mediating flowering, and BES1-BEE1-FT is a new signaling pathway in regulating photoperiodic flowering.

A CRY2-based iTrkB optical strategy induces neurite outgrowth in PC12 cells.

the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling as well as the neurite outgrowth of PC12 cells

A CRY2-based iTrkB optical strategy induces neurite outgrowth in PC12 cells.

the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling as well as the neurite outgrowth of PC12 cells

A CRY2-based iTrkB optical strategy induces neurite outgrowth in PC12 cells.

the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling as well as the neurite outgrowth of PC12 cells

A CRY2-based iTrkB optical strategy induces neurite outgrowth in PC12 cells.

the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling as well as the neurite outgrowth of PC12 cells

A CRY2-based iTrkB optical strategy induces neurite outgrowth in PC12 cells.

the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling as well as the neurite outgrowth of PC12 cells

A CRY2-based iTrkB optical strategy induces neurite outgrowth in PC12 cells.

the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling as well as the neurite outgrowth of PC12 cells

A CRY2-based iTrkB optical strategy induces neurite outgrowth in PC12 cells.

the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling as well as the neurite outgrowth of PC12 cells

BEE1 physically interacts with CRY2 under blue light.

as it physically interacts with CRY2 under the blue light

A CRY2-based iTrkB optical strategy can activate downstream MAPK/ERK and PI3K/Akt signaling.

Utilizing the photosensitive protein Arabidopsis thaliana cryptochrome 2 (CRY2), the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling

A CRY2-based iTrkB optical strategy can activate downstream MAPK/ERK and PI3K/Akt signaling.

Utilizing the photosensitive protein Arabidopsis thaliana cryptochrome 2 (CRY2), the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling

A CRY2-based iTrkB optical strategy can activate downstream MAPK/ERK and PI3K/Akt signaling.

Utilizing the photosensitive protein Arabidopsis thaliana cryptochrome 2 (CRY2), the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling

A CRY2-based iTrkB optical strategy can activate downstream MAPK/ERK and PI3K/Akt signaling.

Utilizing the photosensitive protein Arabidopsis thaliana cryptochrome 2 (CRY2), the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling

A CRY2-based iTrkB optical strategy can activate downstream MAPK/ERK and PI3K/Akt signaling.

Utilizing the photosensitive protein Arabidopsis thaliana cryptochrome 2 (CRY2), the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling

A CRY2-based iTrkB optical strategy can activate downstream MAPK/ERK and PI3K/Akt signaling.

Utilizing the photosensitive protein Arabidopsis thaliana cryptochrome 2 (CRY2), the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling

A CRY2-based iTrkB optical strategy can activate downstream MAPK/ERK and PI3K/Akt signaling.

Utilizing the photosensitive protein Arabidopsis thaliana cryptochrome 2 (CRY2), the light-inducible homo-interaction of the intracellular domain of TrkB (iTrkB) in the cytosol or on the plasma membrane is able to induce the activation of downstream MAPK/ERK and PI3K/Akt signaling

The authors developed different optogenetic approaches that use light to activate TrkB receptors.

Here we develop different optogenetic approaches that use light to activate TrkB receptors.

The authors developed different optogenetic approaches that use light to activate TrkB receptors.

Here we develop different optogenetic approaches that use light to activate TrkB receptors.

The authors developed different optogenetic approaches that use light to activate TrkB receptors.

Here we develop different optogenetic approaches that use light to activate TrkB receptors.

The authors developed different optogenetic approaches that use light to activate TrkB receptors.

Here we develop different optogenetic approaches that use light to activate TrkB receptors.

The authors developed different optogenetic approaches that use light to activate TrkB receptors.

Here we develop different optogenetic approaches that use light to activate TrkB receptors.

The authors developed different optogenetic approaches that use light to activate TrkB receptors.

Here we develop different optogenetic approaches that use light to activate TrkB receptors.

The authors developed different optogenetic approaches that use light to activate TrkB receptors.

Here we develop different optogenetic approaches that use light to activate TrkB receptors.

The paper concerns optogenetic regulation of gene expression in mammalian cells using cryptochrome 2 (CRY2).

The presented optogenetic strategies are promising tools for investigating BDNF/TrkB signaling with tight spatial and temporal control.

The optogenetic strategies presented are promising tools to investigate BDNF/TrkB signaling with tight spatial and temporal control.

The presented optogenetic strategies are promising tools for investigating BDNF/TrkB signaling with tight spatial and temporal control.

The optogenetic strategies presented are promising tools to investigate BDNF/TrkB signaling with tight spatial and temporal control.

The presented optogenetic strategies are promising tools for investigating BDNF/TrkB signaling with tight spatial and temporal control.

The optogenetic strategies presented are promising tools to investigate BDNF/TrkB signaling with tight spatial and temporal control.

The presented optogenetic strategies are promising tools for investigating BDNF/TrkB signaling with tight spatial and temporal control.

The optogenetic strategies presented are promising tools to investigate BDNF/TrkB signaling with tight spatial and temporal control.

The presented optogenetic strategies are promising tools for investigating BDNF/TrkB signaling with tight spatial and temporal control.

The optogenetic strategies presented are promising tools to investigate BDNF/TrkB signaling with tight spatial and temporal control.

The presented optogenetic strategies are promising tools for investigating BDNF/TrkB signaling with tight spatial and temporal control.

The optogenetic strategies presented are promising tools to investigate BDNF/TrkB signaling with tight spatial and temporal control.

The presented optogenetic strategies are promising tools for investigating BDNF/TrkB signaling with tight spatial and temporal control.

The optogenetic strategies presented are promising tools to investigate BDNF/TrkB signaling with tight spatial and temporal control.

CRY2 knockdown increases S phase cell population and reduces G1 phase cell population in HOS osteosarcoma cells.

CRY2 knockdown increased the S phase cell population and reduced the G1 phase cell population.

CRY2 knockdown increases mRNA expression of CRY1, PER1, PER2, BMAL1, and CLOCK in HOS osteosarcoma cells.

knockdown of CRY2 significantly increased the mRNA expression of CRY1, Period (PER) 1, PER2, BMAL1, and CLOCK.

CRY2 may function as an anti-oncogene in osteosarcoma.

Our results suggest that CRY2 may be an anti-oncogene in OS

CRY2 knockdown decreases P53 expression and increases c-myc and cyclin D1 expression in HOS osteosarcoma cells.

CRY2 knockdown decreased P53 expression and increased expression of c-myc and cyclin D1.

CRY2 suppresses proliferation and migration in HOS osteosarcoma cells.

CRY2 knockdown promoted HOS OS cell proliferation and migration.

CRY2 knockdown increases ERK1/2 phosphorylation but does not change JNK and P38 phosphorylation in HOS osteosarcoma cells.

CRY2 knockdown increased the phosphorylation of extracellular signal-regulated kinase (ERK) 1/2, but did not change the phosphorylation of c-Jun N terminal kinase (JNK) and P38.

CRY2 knockdown increases MMP-2 and β-catenin expression and promotes MAPK and Wnt/β-catenin signaling in HOS osteosarcoma cells.

CRY2 knockdown also increased the expression of matrix metalloproteinase (MMP)-2 and β-catenin, and increased OS cell proliferation and migration by inducing cell cycle progression and promoting mitogen-activated protein kinase (MAPK) and Wnt/β-catenin signaling pathways.

The paper presents four strategies for light-inducible activation of TrkA in the absence of NGF.

Here we present the design and evaluation of four strategies for light-inducible activation of TrkA in the absence of NGF. Our strategies involve the light-sensitive protein Arabidopsis cryptochrome 2 and its binding partner CIB1.

CRY1 and CRY2 differ strongly in their blue-light-induced interaction with the COP1/SPA complex.

In total, our results demonstrate that CRY1 and CRY2 strongly differ in their blue light-induced interaction with the COP1/SPA complex.

The blue-light-induced association between CRY2 and COP1 is not dependent on SPA proteins in vivo.

In contrast, the blue light-induced association between CRY2 and COP1 was not dependent on SPA proteins in vivo.

CRY and BIC form a negative-feedback circuitry that regulates each other's activity.

These results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.

CRY2 from Arabidopsis thaliana can be used for blue light-dependent spatiotemporal control of protein homo-oligomerization.

cryptochrome 2 (CRY2) from Arabidopsis thaliana has been recently utilized for blue light-dependent spatiotemporal control of protein homo-oligomerization

Blue light-dependent phosphorylation of the CCE domain determines the photosensitivity of Arabidopsis CRY2.

CRY2 and CIB1 interact upon light illumination.

CRY2 and CIB1, Arabidopsis proteins that interact upon light illumination

CRY1 and CRY2 form a complex with COP1 only after blue-light exposure and not in dark-grown seedlings.

our in vivo co-immunoprecipitation experiments suggest that CRY1 and CRY2 form a complex with COP1 only after seedlings were exposed to blue light. No association between COP1 and CRY1 or CRY2 was observed in dark-grown seedlings.

Arabidopsis cryptochrome 2 undergoes blue light-dependent phosphorylation.

Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2

The nuclear clearing phenotype depended on the presence of a dimerization domain in CRY2-fused transcriptional activators.

The nuclear clearing phenotype was dependent on the presence of a dimerization domain contained within the CRY2-fused transcriptional activators.

The authors identified important determinants for efficient CRY2 clustering.

Here, we identify important determinants for efficient cryptochrome 2 clustering

Cryptochromes activate BIC gene transcription by suppressing COP1 activity, resulting in activation of HY5 associated with chromatins of the BIC promoters.

by suppressing the activity of CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), resulting in activation of the transcription activator ELONGATED HYPOCOTYL 5 (HY5) that is associated with chromatins of the BIC promoters

In mammalian cells, CRY2-tethered proteins showed light-dependent redistribution and clearing within the nucleus.

While adopting this approach to regulate transcription in mammalian cells, we observed light-dependent redistribution and clearing of CRY2-tethered proteins within the nucleus.

Photoreceptor co-action in activating BIC transcription may sustain blue light sensitivity of plants under broad spectra of solar radiation in nature.

suggesting a novel photoreceptor co-action mechanism to sustain blue light sensitivity of plants under the broad spectra of solar radiation in nature.

ΔCC-SPA1 interacts with CRY2 with much lower affinity than wild-type SPA1.

Similarly, ΔCC-SPA1 interacted with CRY2, though with a much lower affinity than wild-type SPA1.

BIC1 and BIC2 inhibit Arabidopsis cryptochrome function by blocking blue light-dependent cryptochrome dimerization.

two negative regulators of Arabidopsis cryptochromes, Blue light Inhibitors of Cryptochromes 1 and 2 (BIC1 and BIC2), inhibit cryptochrome function by blocking blue light-dependent cryptochrome dimerization

This work expands the optogenetic clustering toolbox and provides a guideline for designing new CRY2-based optogenetic modules.

Our work not only expands the optogenetic clustering toolbox but also provides a guideline for designing CRY2-based new optogenetic modules.

Cryptochromes mediate light activation of transcription of the BIC genes.

Here we show that cryptochromes mediate light activation of transcription of the BIC genes

Arabidopsis cryptochrome 2 undergoes blue light-dependent homodimerization to become physiologically active.

We found that Arabidopsis cryptochrome 2 (CRY2) undergoes blue light-dependent homodimerization to become physiologically active.

Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.

Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.

Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.

Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.

Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.

Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.

Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.

Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.

Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.

Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.

Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.

Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.

Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.

Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.

CRY2 mRNA expression in human liver tissue samples was directly associated with hepatic triglyceride content.

In human liver tissue samples, CRY2 mRNA expression was directly associated with hepatic triglyceride content.

CRY2 may act as a switch in hepatic fuel metabolism that promotes triglyceride storage and limits glucose production.

Our data may point to CRY2 as a novel switch in hepatic fuel metabolism promoting triglyceride storage and, concomitantly, limiting glucose production.

Blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele axr6-3, especially under non-permissive temperature.

the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature

Blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele axr6-3, especially under non-permissive temperature.

the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature

Blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele axr6-3, especially under non-permissive temperature.

the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature

Blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele axr6-3, especially under non-permissive temperature.

the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature

Blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele axr6-3, especially under non-permissive temperature.

the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature

Blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele axr6-3, especially under non-permissive temperature.

the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature

Blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele axr6-3, especially under non-permissive temperature.

the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature

Four CRY2 SNPs were associated with fasting glycaemia in non-diabetic individuals.

Four CRY2 SNPs were associated with fasting glycaemia, as reported earlier.

Minor alleles of the CRY2 SNPs associated with fasting glycaemia were associated with elevated fasting glycaemia and reduced liver fat content.

Importantly, carriers of these SNPs' minor alleles revealed elevated fasting glycaemia and, concomitantly, reduced liver fat content.

The authors hypothesize that regulated dimerization governs homeostasis of active cryptochromes in plants and other evolutionary lineages.

We hypothesize that regulated dimerization governs homeostasis of the active cryptochromes in plants and other evolutionary lineages.

Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.

Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3

Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.

Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3

Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.

Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3

Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.

Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3

Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.

Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3

Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.

Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3

Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.

Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3

BIC1 binds to CRY2 and suppresses blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.

We identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.

The role of the COP1-SPA1 complex in blue light-dependent CRY2 degradation is more likely attributable to its CUL4-based E3 ubiquitin ligase activity than to its activity as a cryptochrome signaling partner.

the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner

The role of the COP1-SPA1 complex in blue light-dependent CRY2 degradation is more likely attributable to its CUL4-based E3 ubiquitin ligase activity than to its activity as a cryptochrome signaling partner.

the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner

The role of the COP1-SPA1 complex in blue light-dependent CRY2 degradation is more likely attributable to its CUL4-based E3 ubiquitin ligase activity than to its activity as a cryptochrome signaling partner.

the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner

The role of the COP1-SPA1 complex in blue light-dependent CRY2 degradation is more likely attributable to its CUL4-based E3 ubiquitin ligase activity than to its activity as a cryptochrome signaling partner.

the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner

The role of the COP1-SPA1 complex in blue light-dependent CRY2 degradation is more likely attributable to its CUL4-based E3 ubiquitin ligase activity than to its activity as a cryptochrome signaling partner.

the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner

The role of the COP1-SPA1 complex in blue light-dependent CRY2 degradation is more likely attributable to its CUL4-based E3 ubiquitin ligase activity than to its activity as a cryptochrome signaling partner.

the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner

The role of the COP1-SPA1 complex in blue light-dependent CRY2 degradation is more likely attributable to its CUL4-based E3 ubiquitin ligase activity than to its activity as a cryptochrome signaling partner.

the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner

PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.

Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.

PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.

Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.

PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.

Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.

PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.

Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.

PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.

Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.

PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.

Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.

PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.

Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.

Photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by CUL4- and CUL1-based E3 ubiquitin ligases.

we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4- and CUL1-based E3 ubiquitin ligases

Photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by CUL4- and CUL1-based E3 ubiquitin ligases.

we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4- and CUL1-based E3 ubiquitin ligases

Photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by CUL4- and CUL1-based E3 ubiquitin ligases.

we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4- and CUL1-based E3 ubiquitin ligases

Photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by CUL4- and CUL1-based E3 ubiquitin ligases.

we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4- and CUL1-based E3 ubiquitin ligases

Photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by CUL4- and CUL1-based E3 ubiquitin ligases.

we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4- and CUL1-based E3 ubiquitin ligases

Photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by CUL4- and CUL1-based E3 ubiquitin ligases.

we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4- and CUL1-based E3 ubiquitin ligases

Photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by CUL4- and CUL1-based E3 ubiquitin ligases.

we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4- and CUL1-based E3 ubiquitin ligases

The tested clock gene SNPs were not associated with body fat content, insulin sensitivity, or insulin secretion.

None of the tested SNPs was associated with body fat content, insulin sensitivity, or insulin secretion.

Blue light-dependent CRY2 degradation is only partially impaired in cul4, cop1-5 null, and spa1234 mutants, suggesting involvement of additional E3 ubiquitin ligases.

the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2

Blue light-dependent CRY2 degradation is only partially impaired in cul4, cop1-5 null, and spa1234 mutants, suggesting involvement of additional E3 ubiquitin ligases.

the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2

Blue light-dependent CRY2 degradation is only partially impaired in cul4, cop1-5 null, and spa1234 mutants, suggesting involvement of additional E3 ubiquitin ligases.

the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2

Blue light-dependent CRY2 degradation is only partially impaired in cul4, cop1-5 null, and spa1234 mutants, suggesting involvement of additional E3 ubiquitin ligases.

the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2

Blue light-dependent CRY2 degradation is only partially impaired in cul4, cop1-5 null, and spa1234 mutants, suggesting involvement of additional E3 ubiquitin ligases.

the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2

Blue light-dependent CRY2 degradation is only partially impaired in cul4, cop1-5 null, and spa1234 mutants, suggesting involvement of additional E3 ubiquitin ligases.

the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2

Blue light-dependent CRY2 degradation is only partially impaired in cul4, cop1-5 null, and spa1234 mutants, suggesting involvement of additional E3 ubiquitin ligases.

the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2

Arabidopsis CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

Arabidopsis CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

Arabidopsis CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

Arabidopsis CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

Arabidopsis CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

Arabidopsis CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

Arabidopsis CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation.

ZTL and LKP2 are not required for blue light-dependent CRY2 degradation.

the F-box proteins ZEITLUPE (ZTL) and Lov Kelch Protein2 (LKP2) ... are not required for the blue light-dependent CRY2 degradation

ZTL and LKP2 are not required for blue light-dependent CRY2 degradation.

the F-box proteins ZEITLUPE (ZTL) and Lov Kelch Protein2 (LKP2) ... are not required for the blue light-dependent CRY2 degradation

ZTL and LKP2 are not required for blue light-dependent CRY2 degradation.

the F-box proteins ZEITLUPE (ZTL) and Lov Kelch Protein2 (LKP2) ... are not required for the blue light-dependent CRY2 degradation

ZTL and LKP2 are not required for blue light-dependent CRY2 degradation.

the F-box proteins ZEITLUPE (ZTL) and Lov Kelch Protein2 (LKP2) ... are not required for the blue light-dependent CRY2 degradation

ZTL and LKP2 are not required for blue light-dependent CRY2 degradation.

the F-box proteins ZEITLUPE (ZTL) and Lov Kelch Protein2 (LKP2) ... are not required for the blue light-dependent CRY2 degradation

ZTL and LKP2 are not required for blue light-dependent CRY2 degradation.

the F-box proteins ZEITLUPE (ZTL) and Lov Kelch Protein2 (LKP2) ... are not required for the blue light-dependent CRY2 degradation

ZTL and LKP2 are not required for blue light-dependent CRY2 degradation.

the F-box proteins ZEITLUPE (ZTL) and Lov Kelch Protein2 (LKP2) ... are not required for the blue light-dependent CRY2 degradation

Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.

In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.

Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.

In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.

Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.

In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.

Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.

In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.

Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.

In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.

Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.

In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.

Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.

In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.

The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.

Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.

The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.

Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.

The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.

Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.

The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.

Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.

The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.

Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.

The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.

Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.

The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.

Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.

FBXW7 binds directly to phosphorylated Thr300 of CRY2.

FBXW7 binds directly to phosphorylated Thr300 of CRY2

Upregulation of CRY2 caused by downregulation of FBXW7 may be a novel prognostic biomarker and therapeutic target in colorectal cancer.

Taken together, our findings indicate that the upregulation of CRY2 caused by downregulation of FBXW7 may be a novel prognostic biomarker and may represent a new therapeutic target in colorectal cancer.

CRY2 is a powerful optogenetic tool for light-inducible manipulation of signaling pathways and cellular processes in mammalian cells with high spatiotemporal precision and ease of application.

The photoreceptor cryptochrome 2 (CRY2) has become a powerful optogenetic tool that allows light-inducible manipulation of various signaling pathways and cellular processes in mammalian cells with high spatiotemporal precision and ease of application.

High FBXW7 expression downregulates CRY2 and increases colorectal cancer cell sensitivity to chemotherapy.

High FBXW7 expression downregulates CRY2 and increases colorectal cancer cells' sensitivity to chemotherapy.

Knockdown of CRY2 increases colorectal cancer cell sensitivity to oxaliplatin.

Knockdown of CRY2 increased colorectal cancer sensitivity to oxaliplatin in colorectal cancer cells.

Membrane-bound CRY2 has drastically enhanced oligomerization activity compared with cytoplasmic CRY2.

Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.

Blue light-dependent phosphorylation of the CCE domain determines the photosensitivity of Arabidopsis CRY2.

The Blue Light-Dependent Phosphorylation of the CCE Domain Determines the Photosensitivity of Arabidopsis CRY2

CRY2 is overexpressed in chemoresistant colorectal cancer samples.

Here, we report that CRY2 is overexpressed in chemoresistant colorectal cancer samples

Low FBXW7 expression is correlated with high CRY2 expression in colorectal cancer patient samples.

Low FBXW7 expression is correlated with high CRY2 expression in colorectal cancer patient samples.

CLICR enables optical regulation of target receptor clustering and downstream signalling through noncovalent interactions with engineered Arabidopsis Cry2.

enabled through the optical regulation of target receptor clustering and downstream signalling using noncovalent interactions with engineered Arabidopsis Cryptochrome 2 (Cry2)

Photoexcited CRY2 can undergo both homo-oligomerization and heterodimerization with CIB1 under blue light.

the photoexcited CRY2 can both undergo homo-oligomerization and heterodimerization by binding to its dimerization partner CIB1

Recruitment of cytoplasmic CRY2 to the membrane via interaction with membrane-bound CIB1 significantly intensifies CRY2 homo-oligomerization.

the homo-oligomerization of cytoplasmic CRY2 can be significantly intensified by its recruitment to the membrane via interaction with the membrane-bound CIB1

FBXW7 is a novel E3 ubiquitin ligase that targets CRY2 for proteasomal degradation.

We also identify FBXW7 as a novel E3 ubiquitin ligase for targeting CRY2 through proteasomal degradation.

FBXW7 expression promotes CRY2 degradation by enhancing CRY2 ubiquitination and accelerating CRY2 turnover.

FBXW7 expression leads to degradation of CRY2 through enhancing CRY2 ubiquitination and accelerating the CRY2's turnover rate.

CRY2 overexpression is correlated with poor patient survival in colorectal cancer.

CRY2 overexpression is correlated with poor patient survival

Plant cryptochrome signaling state lifetimes are not, or are only moderately, stabilized in planta relative to other measured contexts.

Thus, the signaling state lifetimes of plant cryptochromes are not, or are only moderately, stabilized in planta.

The in vivo half-life of the signaling state of Arabidopsis cry2 is about 16 minutes.

we estimate the in vivo half-lives of the signaling states of cry1 and cry2 to be in the range of 5 and 16 min, respectively

Although CRY2 physically interacts with CIB1 in response to blue light, CRY2 is not the photoreceptor mediating blue-light suppression of CIB1 degradation.

although cryptochrome 2 physically interacts with CIB1 in response to blue light, it is not the photoreceptor mediating blue-light suppression of CIB1 degradation

Cryptochrome and LOV-domain F-box proteins mediate blue-light regulation of the same transcription factor, CIB1, by distinct mechanisms.

These results support the hypothesis that the evolutionarily unrelated blue-light receptors, cryptochrome and LOV-domain F-box proteins, mediate blue-light regulation of the same transcription factor by distinct mechanisms.

Photoexcited CRY2 interacts with the transcription factor CIB1 in Arabidopsis in response to blue light.

In Arabidopsis, the photoexcited cryptochrome 2 interacts with the transcription factor CRYPTOCHROME-INTERACTING basic helix-loop-helix 1 (CIB1)

The paper describes development of LITEs, an optogenetic two-hybrid system integrating a TALE DNA-binding domain with cryptochrome 2 and CIB1.

Here we describe the development of light-inducible transcriptional effectors (LITEs), an optogenetic two-hybrid system integrating the customizable TALE DNA-binding domain with the light-sensitive cryptochrome 2 protein and its interacting partner CIB1 from Arabidopsis thaliana.

phyA influences cry2 stability because a phyA mutant has enhanced cry2 levels, particularly under low fluence rate blue light.

a phyA mutant had enhanced cry2 levels, particularly under low fluence rate blue light

phyA influences cry2 stability because a phyA mutant has enhanced cry2 levels, particularly under low fluence rate blue light.

a phyA mutant had enhanced cry2 levels, particularly under low fluence rate blue light

phyA influences cry2 stability because a phyA mutant has enhanced cry2 levels, particularly under low fluence rate blue light.

a phyA mutant had enhanced cry2 levels, particularly under low fluence rate blue light

phyA influences cry2 stability because a phyA mutant has enhanced cry2 levels, particularly under low fluence rate blue light.

a phyA mutant had enhanced cry2 levels, particularly under low fluence rate blue light

phyA influences cry2 stability because a phyA mutant has enhanced cry2 levels, particularly under low fluence rate blue light.

a phyA mutant had enhanced cry2 levels, particularly under low fluence rate blue light

phyA influences cry2 stability because a phyA mutant has enhanced cry2 levels, particularly under low fluence rate blue light.

a phyA mutant had enhanced cry2 levels, particularly under low fluence rate blue light

phyA influences cry2 stability because a phyA mutant has enhanced cry2 levels, particularly under low fluence rate blue light.

a phyA mutant had enhanced cry2 levels, particularly under low fluence rate blue light

SPA proteins contribute to cry2 degradation because cry2 degradation under continuous blue light is alleviated in spa mutants in a fluence rate-dependent manner.

In all spa mutants analyzed, cry2 degradation under continuous blue light was alleviated in a fluence rate-dependent manner.

SPA proteins contribute to cry2 degradation because cry2 degradation under continuous blue light is alleviated in spa mutants in a fluence rate-dependent manner.

In all spa mutants analyzed, cry2 degradation under continuous blue light was alleviated in a fluence rate-dependent manner.

SPA proteins contribute to cry2 degradation because cry2 degradation under continuous blue light is alleviated in spa mutants in a fluence rate-dependent manner.

In all spa mutants analyzed, cry2 degradation under continuous blue light was alleviated in a fluence rate-dependent manner.

SPA proteins contribute to cry2 degradation because cry2 degradation under continuous blue light is alleviated in spa mutants in a fluence rate-dependent manner.

In all spa mutants analyzed, cry2 degradation under continuous blue light was alleviated in a fluence rate-dependent manner.

SPA proteins contribute to cry2 degradation because cry2 degradation under continuous blue light is alleviated in spa mutants in a fluence rate-dependent manner.

In all spa mutants analyzed, cry2 degradation under continuous blue light was alleviated in a fluence rate-dependent manner.

SPA proteins contribute to cry2 degradation because cry2 degradation under continuous blue light is alleviated in spa mutants in a fluence rate-dependent manner.

In all spa mutants analyzed, cry2 degradation under continuous blue light was alleviated in a fluence rate-dependent manner.

SPA proteins contribute to cry2 degradation because cry2 degradation under continuous blue light is alleviated in spa mutants in a fluence rate-dependent manner.

In all spa mutants analyzed, cry2 degradation under continuous blue light was alleviated in a fluence rate-dependent manner.

cry2 stability is controlled by SPA and phyA.

Our results suggest that cry2 stability is controlled by SPA and phyA

cry2 stability is controlled by SPA and phyA.

Our results suggest that cry2 stability is controlled by SPA and phyA

cry2 stability is controlled by SPA and phyA.

Our results suggest that cry2 stability is controlled by SPA and phyA

cry2 stability is controlled by SPA and phyA.

Our results suggest that cry2 stability is controlled by SPA and phyA

cry2 stability is controlled by SPA and phyA.

Our results suggest that cry2 stability is controlled by SPA and phyA

cry2 stability is controlled by SPA and phyA.

Our results suggest that cry2 stability is controlled by SPA and phyA

cry2 stability is controlled by SPA and phyA.

Our results suggest that cry2 stability is controlled by SPA and phyA

cry2 physically interacts with SPA1 in nuclei of living cells.

Fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy studies showed a robust physical interaction of cry2 with SPA1 in nuclei of living cells.

cry2 physically interacts with SPA1 in nuclei of living cells.

Fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy studies showed a robust physical interaction of cry2 with SPA1 in nuclei of living cells.

cry2 physically interacts with SPA1 in nuclei of living cells.

Fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy studies showed a robust physical interaction of cry2 with SPA1 in nuclei of living cells.

cry2 physically interacts with SPA1 in nuclei of living cells.

Fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy studies showed a robust physical interaction of cry2 with SPA1 in nuclei of living cells.

cry2 physically interacts with SPA1 in nuclei of living cells.

Fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy studies showed a robust physical interaction of cry2 with SPA1 in nuclei of living cells.

cry2 physically interacts with SPA1 in nuclei of living cells.

Fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy studies showed a robust physical interaction of cry2 with SPA1 in nuclei of living cells.

cry2 physically interacts with SPA1 in nuclei of living cells.

Fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy studies showed a robust physical interaction of cry2 with SPA1 in nuclei of living cells.

In etiolated Arabidopsis seedlings exposed to blue light, cry2 protein level strongly decreases and cry2 is phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

The cry2 protein level strongly decreases when etiolated seedlings are exposed to blue light; cry2 is first phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

In etiolated Arabidopsis seedlings exposed to blue light, cry2 protein level strongly decreases and cry2 is phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

The cry2 protein level strongly decreases when etiolated seedlings are exposed to blue light; cry2 is first phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

In etiolated Arabidopsis seedlings exposed to blue light, cry2 protein level strongly decreases and cry2 is phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

The cry2 protein level strongly decreases when etiolated seedlings are exposed to blue light; cry2 is first phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

In etiolated Arabidopsis seedlings exposed to blue light, cry2 protein level strongly decreases and cry2 is phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

The cry2 protein level strongly decreases when etiolated seedlings are exposed to blue light; cry2 is first phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

In etiolated Arabidopsis seedlings exposed to blue light, cry2 protein level strongly decreases and cry2 is phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

The cry2 protein level strongly decreases when etiolated seedlings are exposed to blue light; cry2 is first phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

In etiolated Arabidopsis seedlings exposed to blue light, cry2 protein level strongly decreases and cry2 is phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

The cry2 protein level strongly decreases when etiolated seedlings are exposed to blue light; cry2 is first phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

In etiolated Arabidopsis seedlings exposed to blue light, cry2 protein level strongly decreases and cry2 is phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

The cry2 protein level strongly decreases when etiolated seedlings are exposed to blue light; cry2 is first phosphorylated, polyubiquitinated, and then degraded by the 26S proteasome.

The blue light-induced transcription system used in this study is based on the blue light-dependent interaction between CRY2 and CIB1.

Here we exploited the blue light-induced transcription system in yeast and zebrafish, based on the blue light dependent interaction between two plant proteins, blue light photoreceptor Cryptochrome 2 (CRY2) and the bHLH transcription factor CIB1 (CRY-interacting bHLH 1).

CRY2 trp-triad mutations tested lost photoreduction activity in vitro but retained physiological and biochemical activities in vivo.

We found that all trp-triad mutations of CRY2 tested lost photoreduction activity in vitro but retained the physiological and biochemical activities in vivo.

The trp-triad residues are evolutionarily conserved in the photolyase/cryptochrome superfamily for structural integrity rather than for photochemistry per se.

the trp-triad residues are evolutionarily conserved in the photolyase/cryptochrome superfamily for reasons of structural integrity rather than for photochemistry per se

Some trp-triad mutations of CRY2 remained responsive to blue light, whereas CRY2(W374A) became constitutively active.

Some of the trp-triad mutations of CRY2 remained responsive to blue light; others, such as CRY2(W374A), became constitutively active.

Arabidopsis CRY2 functions by a photoactivation mechanism distinct from trp-triad-dependent photoreduction.

These results support the hypothesis that cryptochromes mediate blue-light responses via a photochemistry distinct from trp-triad-dependent photoreduction

Wild-type CRY2 undergoes blue-light-dependent interaction with SPA1 and CIB1, whereas CRY2(W374A) interacts with SPA1 and CIB1 constitutively.

In contrast to wild-type CRY2, which undergoes blue-light-dependent interaction with the CRY2-signaling proteins SUPPRESSOR OF PHYA 1 (SPA1) and cryptochrome-interaction basic helix-loop-helix 1 (CIB1), the constitutively active CRY2(W374A) interacts with SPA1 and CIB1 constitutively.

Exposure to darkness or blue light induces degradation of CRY2 and subsequently HRT, resulting in susceptibility.

Exposure to darkness or blue-light induces degradation of CRY2, and in turn HRT, resulting in susceptibility.

CRY2 and PHOT2 are required for HRT stability and thereby resistance to Turnip Crinkle virus.

The blue-light photoreceptors, cryptochrome (CRY) 2 and phototropin (PHOT) 2, are required for the stability of the R protein HRT, and thereby resistance to Turnip Crinkle virus (TCV).

HRT overexpression compensates for absence of PHOT2 but not absence of CRY2.

Overexpression of HRT can compensate for the absence of PHOT2 but not CRY2.

CRY2 and PHOT2 negatively regulate proteasome-mediated degradation of HRT, likely via COP1, and blue light relieves this repression resulting in HRT degradation.

We propose that CRY2/PHOT2 negatively regulate the proteasome-mediated degradation of HRT, likely via COP1, and blue-light relieves this repression resulting in HRT degradation.

HRT does not directly associate with CRY2 or PHOT2 but does bind COP1.

HRT does not directly associate with either CRY2 or PHOT2 but does bind the CRY2-/PHOT2-interacting E3 ubiquitin ligase, COP1.

Aedes aegypti and Culex quinquefasciatus show conserved circadian expression patterns for all major cycling clock genes except cry2.

they show conserved circadian expression patterns for all major cycling clock genes except mammalian-like cryptochrome2 (cry2)

Aedes aegypti and Culex quinquefasciatus show conserved circadian expression patterns for all major cycling clock genes except cry2.

they show conserved circadian expression patterns for all major cycling clock genes except mammalian-like cryptochrome2 (cry2)

Aedes aegypti and Culex quinquefasciatus show conserved circadian expression patterns for all major cycling clock genes except cry2.

they show conserved circadian expression patterns for all major cycling clock genes except mammalian-like cryptochrome2 (cry2)

Aedes aegypti and Culex quinquefasciatus show conserved circadian expression patterns for all major cycling clock genes except cry2.

they show conserved circadian expression patterns for all major cycling clock genes except mammalian-like cryptochrome2 (cry2)

Aedes aegypti and Culex quinquefasciatus show conserved circadian expression patterns for all major cycling clock genes except cry2.

they show conserved circadian expression patterns for all major cycling clock genes except mammalian-like cryptochrome2 (cry2)

Aedes aegypti and Culex quinquefasciatus show conserved circadian expression patterns for all major cycling clock genes except cry2.

they show conserved circadian expression patterns for all major cycling clock genes except mammalian-like cryptochrome2 (cry2)

Aedes aegypti and Culex quinquefasciatus show conserved circadian expression patterns for all major cycling clock genes except cry2.

they show conserved circadian expression patterns for all major cycling clock genes except mammalian-like cryptochrome2 (cry2)

CRY2-GFP degradation is significantly retarded in response to blue light compared with GFP-CRY2 or endogenous CRY2.

Compared with GFP-CRY2 or the endogenous CRY2, CRY2-GFP degradation was significantly retarded in response to blue light

GFP-CRY2 exhibits light-dependent biochemical and physiological activities similar to endogenous CRY2.

While GFP-CRY2 exerts light-dependent biochemical and physiological activities similar to those of the endogenous CRY2

Differences in cry2 mRNA profiles correlate with behavioral differences between Aedes aegypti and Culex quinquefasciatus and suggest a potential role for cry2 in species-specific rhythmic behavior.

the correlation between the differences in behavior between Ae. aegypti and Cx. quinquefasciatus and their corresponding cry2 mRNA profiles suggests a potential role for this clock gene in controlling species-specific rhythmic behavior

Differences in cry2 mRNA profiles correlate with behavioral differences between Aedes aegypti and Culex quinquefasciatus and suggest a potential role for cry2 in species-specific rhythmic behavior.

the correlation between the differences in behavior between Ae. aegypti and Cx. quinquefasciatus and their corresponding cry2 mRNA profiles suggests a potential role for this clock gene in controlling species-specific rhythmic behavior

Differences in cry2 mRNA profiles correlate with behavioral differences between Aedes aegypti and Culex quinquefasciatus and suggest a potential role for cry2 in species-specific rhythmic behavior.

the correlation between the differences in behavior between Ae. aegypti and Cx. quinquefasciatus and their corresponding cry2 mRNA profiles suggests a potential role for this clock gene in controlling species-specific rhythmic behavior

Differences in cry2 mRNA profiles correlate with behavioral differences between Aedes aegypti and Culex quinquefasciatus and suggest a potential role for cry2 in species-specific rhythmic behavior.

the correlation between the differences in behavior between Ae. aegypti and Cx. quinquefasciatus and their corresponding cry2 mRNA profiles suggests a potential role for this clock gene in controlling species-specific rhythmic behavior

Differences in cry2 mRNA profiles correlate with behavioral differences between Aedes aegypti and Culex quinquefasciatus and suggest a potential role for cry2 in species-specific rhythmic behavior.

the correlation between the differences in behavior between Ae. aegypti and Cx. quinquefasciatus and their corresponding cry2 mRNA profiles suggests a potential role for this clock gene in controlling species-specific rhythmic behavior

Differences in cry2 mRNA profiles correlate with behavioral differences between Aedes aegypti and Culex quinquefasciatus and suggest a potential role for cry2 in species-specific rhythmic behavior.

the correlation between the differences in behavior between Ae. aegypti and Cx. quinquefasciatus and their corresponding cry2 mRNA profiles suggests a potential role for this clock gene in controlling species-specific rhythmic behavior

Differences in cry2 mRNA profiles correlate with behavioral differences between Aedes aegypti and Culex quinquefasciatus and suggest a potential role for cry2 in species-specific rhythmic behavior.

the correlation between the differences in behavior between Ae. aegypti and Cx. quinquefasciatus and their corresponding cry2 mRNA profiles suggests a potential role for this clock gene in controlling species-specific rhythmic behavior

The results are consistent with the hypothesis that photoexcited CRY2 disengages its C-terminal domain from the PHR domain to become active.

These results are consistent with the hypothesis that photoexcited CRY2 disengages its C-terminal domain from the PHR domain to become active.

Different mechanisms for cry2 regulation may exist in Aedes aegypti and Culex quinquefasciatus.

The results indicate that different mechanisms for cry2 regulation may exist for the two species.

Different mechanisms for cry2 regulation may exist in Aedes aegypti and Culex quinquefasciatus.

The results indicate that different mechanisms for cry2 regulation may exist for the two species.

Different mechanisms for cry2 regulation may exist in Aedes aegypti and Culex quinquefasciatus.

The results indicate that different mechanisms for cry2 regulation may exist for the two species.

Different mechanisms for cry2 regulation may exist in Aedes aegypti and Culex quinquefasciatus.

The results indicate that different mechanisms for cry2 regulation may exist for the two species.

Different mechanisms for cry2 regulation may exist in Aedes aegypti and Culex quinquefasciatus.

The results indicate that different mechanisms for cry2 regulation may exist for the two species.

Different mechanisms for cry2 regulation may exist in Aedes aegypti and Culex quinquefasciatus.

The results indicate that different mechanisms for cry2 regulation may exist for the two species.

Different mechanisms for cry2 regulation may exist in Aedes aegypti and Culex quinquefasciatus.

The results indicate that different mechanisms for cry2 regulation may exist for the two species.

Both GFP-CRY2 and endogenous CRY2 form nuclear bodies in the presence of 26S-proteasome inhibitors that block blue light-dependent CRY2 degradation.

we showed that both GFP-CRY2 and endogenous CRY2 formed nuclear bodies in the presence of the 26S-proteasome inhibitors that block blue light-dependent CRY2 degradation

CIB1 acts together with additional CIB1-related proteins to promote CRY2-dependent floral initiation.

it acts together with additional CIB1-related proteins to promote CRY2-dependent floral initiation

CIB1 interacts with CRY2 in a blue light-specific manner.

CIB1 interacts with CRY2 (cryptochrome 2) in a blue light-specific manner in yeast and Arabidopsis cells

Blue light-dependent interaction of cryptochrome(s) with CIB1 and CIB1-related proteins represents an early photoreceptor signaling mechanism in plants.

We propose that the blue light-dependent interaction of cryptochrome(s) with CIB1 and CIB1-related proteins represents an early photoreceptor signaling mechanism in plants.

The active form of Cry2 contains FADH(.) rather than the fully reduced flavin state required for catalytically active photolyase.

These results demonstrate that the active form of Cry2 contains FADH(.) (whereas catalytically active photolyase requires fully reduced flavin (FADH(-))).

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.

The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated

At least two rounds of gene duplication at the base of the metazoan radiation, together with several losses, gave rise to two cryptochrome gene families in insects: a Drosophila-like cry1 family and a vertebrate-like cry2 family.

Phylogenetic analyses show at least 2 rounds of gene duplication at the base of the metazoan radiation, as well as several losses, gave rise to 2 cryptochrome (cry) gene families in insects, a Drosophila-like cry1 gene family and a vertebrate-like cry2 family.

The transcriptional repressive function of insect CRY2 descended from a light-sensitive photolyase-like ancestral gene that probably lacked the ability to repress CLOCK:CYCLE-mediated transcription.

By mapping the functional data onto a cryptochrome/6-4 photolyase gene tree, we find that the transcriptional repressive function of insect CRY2 descended from a light-sensitive photolyase-like ancestral gene, probably lacking the ability to repress CLOCK:CYCLE-mediated transcription.

Cryptochromes may use flavin redox states for signaling differently from DNA-photolyase for photorepair.

suggest that cryptochromes could represent photoreceptors using flavin redox states for signaling differently from DNA-photolyase for photorepair

This study extended the transcriptional repressive function of insect CRY2 to Hymenoptera and Coleoptera, including Apis mellifera, Bombus impatiens, and Tribolium castaneum.

Here, we extended the transcriptional repressive function of insect CRY2 to 2 orders--Hymenoptera (the honeybee Apis mellifera and the bumblebee Bombus impatiens) and Coleoptera (the red flour beetle Tribolium castaneum).

Previous studies showed that insect CRY1 is photosensitive, whereas photo-insensitive CRY2 potently inhibits CLOCK:CYCLE-mediated transcription.

Previous studies have shown that insect CRY1 is photosensitive, whereas photo-insensitive CRY2 functions to potently inhibit clock-relevant CLOCK:CYCLE-mediated transcription.

The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.

Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.

The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.

Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.

The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.

Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.

The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.

Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.

The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.

Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.

The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.

Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.

The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.

Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.

Green light irradiation of Cry2 changes the equilibrium of flavin oxidation states and attenuates Cry2-controlled responses such as flowering.

Green light irradiation of Cry2 causes a change in the equilibrium of flavin oxidation states and attenuates Cry2-controlled responses such as flowering.

Bee and beetle CRY2 proteins are not light sensitive in culture, in either protein degradation or inhibitory transcriptional response.

Importantly, the bee and beetle CRY2 proteins are not light sensitive in culture, in either degradation of protein levels or inhibitory transcriptional response

Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.

suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif

Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.

suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif

Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.

suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif

Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.

suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif

Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.

suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif

Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.

suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif