Source 1primary paper2015ACS Synthetic Biology
Toolkit/CRY2/CIB1
CRY2/CIB1
Also known as: CRY2/CIB, CRY2-CIB1, CRY2/CIB1, CRY2-CIB dimerizer, CRY2-CIB dimerizers, cryptochrome2 (CRY2)/CIB1, cryptochrome 2 system
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
CRY2/CIB1 is a blue-light-inducible multi-component interaction switch composed of the photoreceptor CRY2 and its interacting partner CIB1. It is used for acute light-dependent protein recruitment, including plasma-membrane recruitment and clustering, to control protein localization and downstream signaling with high spatial and temporal resolution.
Usefulness & Problems
Why this is useful
This system enables optical control of protein localization and activity with high spatial and temporal resolution in cellular optogenetics. In the cited fission yeast studies, it supported acute recruitment of Cdc42 variants to the plasma membrane and thereby enabled perturbation of polarity signaling.
Source:
Here, we use the CRY2-CIB1 optogenetic system to recruit and cluster a cytosolic Cdc42 allele at the plasma membrane and show that this leads to its moderate activation also on cell sides.
Source:
Here, we use the CRY2-CIB1 optogenetic system to recruit and cluster a cytosolic Cdc42 variant at the plasma membrane and show that this leads to its moderate activation also on cell sides.
Source:
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Source:
The improvements regarding the FKF1/GI- and CRY2/CIB1-based systems will be widely applicable for the light-dependent control of transcription in mammalian cells.
Problem solved
CRY2/CIB1 addresses the need for reversible, light-gated control of intracellular protein positioning and signaling without constitutive tethering. The supplied evidence specifically supports its use for plasma-membrane recruitment and clustering of cytosolic proteins to probe Cdc42-dependent polarization mechanisms.
Source:
The improvements regarding the FKF1/GI- and CRY2/CIB1-based systems will be widely applicable for the light-dependent control of transcription in mammalian cells.
Source:
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
Problem links
Need conditional control of signaling activity
DerivedCRY2/CIB1 is a blue-light-inducible multi-component interaction switch built from the photoreceptor CRY2 and its interacting partner CIB1. It is used to drive acute light-dependent protein recruitment, including plasma-membrane recruitment and clustering, to control localization and downstream signaling with high spatial and temporal resolution.
Need conditional recombination or state switching
DerivedCRY2/CIB1 is a blue-light-inducible multi-component interaction switch built from the photoreceptor CRY2 and its interacting partner CIB1. It is used to drive acute light-dependent protein recruitment, including plasma-membrane recruitment and clustering, to control localization and downstream signaling with high spatial and temporal resolution.
Need inducible protein relocalization or recruitment
DerivedCRY2/CIB1 is a blue-light-inducible multi-component interaction switch built from the photoreceptor CRY2 and its interacting partner CIB1. It is used to drive acute light-dependent protein recruitment, including plasma-membrane recruitment and clustering, to control localization and downstream signaling with high spatial and temporal resolution.
Need precise spatiotemporal control with light input
DerivedCRY2/CIB1 is a blue-light-inducible multi-component interaction switch built from the photoreceptor CRY2 and its interacting partner CIB1. It is used to drive acute light-dependent protein recruitment, including plasma-membrane recruitment and clustering, to control localization and downstream signaling with high spatial and temporal resolution.
Need tighter control over gene expression timing or amplitude
DerivedCRY2/CIB1 is a blue-light-inducible multi-component interaction switch built from the photoreceptor CRY2 and its interacting partner CIB1. It is used to drive acute light-dependent protein recruitment, including plasma-membrane recruitment and clustering, to control localization and downstream signaling with high spatial and temporal resolution.
Workflow Fit
Likely fit
- •fast-no-cloning-screen: useful for quick interaction-switch feasibility checks
- •standard-construct-loop: useful when localization, stoichiometry, or effector fusion details need iteration
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
HeterodimerizationHeterodimerizationHeterodimerizationOligomerizationOligomerizationOligomerizationTarget processes
localizationrecombinationsignalingtranscriptionInput: Light
Output: Signaling
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementmechanism class: light-dependent bindingoperating role: actuatoroperating role: regulatorphotoreceptor family: cryptochromeswitch architecture: multi componentswitch architecture: recruitmentswitch architecture: split
The system consists of the photoreceptor CRY2 and its interacting partner CIB1 and is activated by blue light. Reported implementations used it to recruit and cluster cytosolic Cdc42 variants or alleles at the plasma membrane in Schizosaccharomyces pombe, implying a two-component construct design with one partner positioned for cortical recruitment.
The provided evidence indicates that CRY2/CIB1 properties vary dramatically in dark-state and lit-state binding affinity relative to other dimerizers, but it does not provide quantitative values here. Validation in the supplied claims is concentrated on localization and signaling assays in fission yeast, so broader organismal performance, kinetics, and photophysical constraints are not established from this evidence set alone.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Observations
successYeastmechanistic demoSchizosaccharomyces pombe
Inferred from claim c2 during normalization. Optogenetic recruitment of constitutively active Cdc42 leads to co-recruitment of Scd1 and endogenous Cdc42 in a Scd2-dependent manner. Derived from claim c2. Quoted text: optogenetic recruitment of constitutively active Cdc42 leads to co-recruitment of the guanine nucleotide exchange factor (GEF) Scd1 and endogenous Cdc42, in a manner dependent on the scaffold protein Scd2
Source:
successYeastapplication demoSchizosaccharomyces pombe
Inferred from claim c1 during normalization. The CRY2-CIB1 optogenetic system was used to recruit and cluster a cytosolic Cdc42 allele at the plasma membrane, leading to moderate activation on cell sides. Derived from claim c1. Quoted text: Here, we use the CRY2-CIB1 optogenetic system to recruit and cluster a cytosolic Cdc42 allele at the plasma membrane and show that this leads to its moderate activation also on cell sides.
Source:
Supporting Sources
Source 2primary paper2019Figshare
Source 3primary paper2018Proceedings of the National Academy of Sciences
Source 4primary paper2016Nature Chemical Biology
Source 5review2017Journal of Experimental Neuroscience
Source 6review2014Biotechnology Journal
Source 7primary paper2020PLoS Biology
Source 8primary paper2020
Source 9primary paper2020Cells
Source 10primary paper2017Nucleic Acids Research
Source 11primary paper2014ACS Synthetic Biology
Ranked Claims
Scaffold-mediated positive feedback gated by Ras activity confers robust polarization for rod-shape formation.
We conclude that scaffold-mediated positive feedback, gated by Ras activity, confers robust polarization for rod-shape formation.
The study implemented the CRY2-CIB1 optogenetic system for acute light-dependent protein recruitment to the plasma membrane in Schizosaccharomyces pombe.
We implemented the CRY2-CIB1 optogenetic system for acute light-dependent protein recruitment to the plasma membrane
Optogenetic recruitment of constitutively active Cdc42 leads to co-recruitment of Scd1 and endogenous Cdc42 in a Scd2-dependent manner.
optogenetic recruitment of constitutively active Cdc42 leads to co-recruitment of the guanine nucleotide exchange factor (GEF) Scd1 and endogenous Cdc42, in a manner dependent on the scaffold protein Scd2
The CRY2-CIB1 optogenetic system was used to recruit and cluster a cytosolic Cdc42 allele at the plasma membrane, leading to moderate activation on cell sides.
Here, we use the CRY2-CIB1 optogenetic system to recruit and cluster a cytosolic Cdc42 allele at the plasma membrane and show that this leads to its moderate activation also on cell sides.
Using the CRY2-CIB1 optogenetic system to recruit and cluster a cytosolic Cdc42 variant at the plasma membrane leads to moderate Cdc42 activation on cell sides.
Here, we use the CRY2-CIB1 optogenetic system to recruit and cluster a cytosolic Cdc42 variant at the plasma membrane and show that this leads to its moderate activation also on cell sides.
Section: abstract
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.
Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.
The optimized FKF1/GI- and CRY2/CIB1-based systems are presented as widely applicable for light-dependent control of transcription in mammalian cells.
The improvements regarding the FKF1/GI- and CRY2/CIB1-based systems will be widely applicable for the light-dependent control of transcription in mammalian cells.
CRY2/CIB1-based light-inducible transcription was improved by split construct optimization in mammalian cells.
In addition, we have improved the CRY2/CIB1-based light-inducible transcription with split construct optimization.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports optimized second-generation CRY2–CIB dimerizers.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The paper reports a photoactivatable Cre recombinase.
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
Photoreceptor-based optogenetic tools in this review rely on light-dependent reversible binding to specific interaction partners.
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
Approval Evidence
9 sources19 linked approval claimsfirst-pass slugs cry2-cib1, cry2-cib-dimerizers
the photoreceptor CRY2 and its interacting partner CIB1 plasmid
Source:
three blue-light-inducible dimer variants (cryptochrome2 (CRY2)/CIB1, iLID/SspB, and LOVpep/ePDZb)
Source:
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Source:
Explicitly supported in the supplied web research summary as a named optogenetic interaction module aligned with the review scope.
Source:
Optimized second-generation CRY2–CIB dimerizers and photoactivatable Cre recombinase
Source:
three blue-light-inducible dimer variants (cryptochrome2 (CRY2)/CIB1, iLID/SspB, and LOVpep/ePDZb)
Source:
The supplied source summary states that the review frames optimization around major photosensory modules including CRY2/CIB1.
Source:
Here, we set about to systematically benchmark the properties of four optical dimerizer systems, CRY2/CIB1, TULIPs, phyB/PIF3, and phyB/PIF6.
Source:
These tools are based on photoreceptors such as ... cryptochrome 2 ... that reversibly bind to specific interaction partners in a light-dependent manner.
Source:
application demonstrationsupports
Camouflage nanoparticle-based vectors were demonstrated for in situ bioluminescence-driven optogenetic therapy of retinoblastoma.
Herein, we present the demonstration of camouflage nanoparticle-based vectors for in situ bioluminescence-driven optogenetic therapy of retinoblastoma. To conduct proof-of-concept research, this study employs a mouse model of retinoblastoma.
Source:
comparative efficacysupports
Compared with external blue light irradiation, the developed system inhibited tumor growth with greater therapeutic efficacy and significantly reduced ocular tumor size.
In comparison to external blue light irradiation, the developed system enables an in situ bioluminescence-activated apoptotic pathway to inhibit tumor growth with greater therapeutic efficacy, resulting in a significant reduction in ocular tumor size.
Source:
safety comparisonsupports
Unlike external blue light irradiation, the camouflage nanoparticle-based optogenetic system maintained retinal structural integrity and avoided corneal neovascularization.
Furthermore, unlike external blue light irradiation, which causes retinal damage and corneal neovascularization, the camouflage nanoparticle-based optogenetic system maintains retinal structural integrity while avoiding corneal neovascularization.
Source:
capabilitysupports
Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.
Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.
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comparative propertysupports
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
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correlationsupports
Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.
we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...
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comparative performancesupports
Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
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determinant of spatial confinementsupports
The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.
We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.
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optimization reportsupports
The paper reports optimized second-generation CRY2–CIB dimerizers.
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assay applicationsupports
The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.
in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
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comparative characterizationsupports
CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.
We find that the switches vary dramatically in their dark and lit state binding affinities
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correlationsupports
Binding affinities of the examined blue-light-inducible dimers correlate with activity changes in in vivo assays.
these affinities correlate with activity changes in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling
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mechanistic effectsupports
For CRY2, light-induced changes in homo-oligomerization can significantly affect activity and are sensitive to alternative fusion strategies.
Additionally, for CRY2, we observe that light-induced changes in homo-oligomerization can have significant effects on activity that are sensitive to alternative fusion strategies.
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module family coveragesupports
The review covers CRY2/CIB1, LOV-domain systems, phytochrome/PIF systems, and Dronpa-based designs as major photosensory modules relevant to optogenetic construct optimization.
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application demosupports
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
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background activity comparisonsupports
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
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benchmark resultsupports
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
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mechanism summarysupports
Photoreceptor-based optogenetic tools in this review rely on light-dependent reversible binding to specific interaction partners.
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pathway regulation comparisonsupports
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
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Comparisons
Source-backed strengths
The tool is explicitly described as a blue-light-inducible dimer system and as one of several optical dimerizers benchmarked in vitro and in vivo. It has been used in Schizosaccharomyces pombe for acute plasma-membrane recruitment, where recruitment and clustering of cytosolic Cdc42 alleles produced moderate activation on cell sides, and the broader literature cited includes optimized second-generation CRY2-CIB dimerizers.
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We find that the switches vary dramatically in their dark and lit state binding affinities
Source:
Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.
Source:
The paper reports optimized second-generation CRY2–CIB dimerizers.
Source:
We find that the switches vary dramatically in their dark and lit state binding affinities
Compared with iLID/SspB
CRY2/CIB1 and iLID/SspB address a similar problem space because they share localization, recombination, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, recombination, signaling, transcription; shared mechanisms: heterodimerization; same primary input modality: light
Compared with LOVpep/ePDZb
CRY2/CIB1 and LOVpep/ePDZb address a similar problem space because they share localization, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, signaling, transcription; shared mechanisms: heterodimerization; same primary input modality: light
Strengths here: appears more independently replicated.
CRY2/CIB1 and single-component optogenetic tools for inducible RhoA GTPase signaling address a similar problem space because they share localization, recombination, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, recombination, signaling, transcription; shared mechanisms: heterodimerization; same primary input modality: light
Strengths here: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
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Curation Status
Seed dossier — not yet curator-complete
- Validation rollups and replication scores are pending ingestion
- Citation list may be incomplete or contain placeholders
- Observation table will populate once evidence is curated