Toolkit/CRY2/CIB1

CRY2/CIB1

Multi-Component Switch·cryptochrome·Research·Since 2014Seed — needs curation

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.

Assembly Hierarchy

Components

  • CIB1protein domain
  • Cry2multi component switch

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

Published Workflows

Optogenetic Modulation of Intracellular Signalling and Transcription: Focus on Neuronal Plasticity

2017

Objective: Deploy optogenetic photo-actuators in vivo to modulate intracellular signalling and transcription for studying neuronal plasticity.

light-responsive modulation of intracellular signallinglight-responsive modulation of transcriptionoptogenetic engineeringin vivo expressionlight stimulation

Stages

  1. 1.
    In vivo expression of photo-actuators(functional_characterization)

    The abstract explicitly notes that successful in vivo expression is a required process before systems-level use.

    Selection: successful expression of photo-actuators in vivo

  2. 2.
    In vivo stimulation of photo-actuators(confirmatory_validation)

    The abstract states that stimulation is a required process for successful in vivo use after expression.

    Selection: successful stimulation of expressed photo-actuators in vivo

  3. 3.
    Systems-level application to neuronal plasticity(in_vivo_validation)

    The abstract frames neuronal plasticity understanding as the downstream application after successful in vivo expression and stimulation.

    Selection: use of successfully deployed optogenetic tools to study neuronal plasticity at the systems level

Taxonomy & Function

Primary hierarchy

Mechanism Branch

Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.

Target processes

localizationrecombinationsignalingtranscription

Input: Light

Output: Signaling

Implementation Constraints

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

Ranked Claims

Claim 1conclusionsupports2020Source 7needs review

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.
Claim 2implementationsupports2020Source 7needs review

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
Claim 3mechanismsupports2020Source 7needs review

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
Claim 4tool effectsupports2020Source 8needs review

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.
Claim 5tool effectsupports2020Source 9needs review

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
Claim 6capabilitysupports2019Source 2needs review

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.
Claim 7capabilitysupports2019Source 2needs review

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.
Claim 8capabilitysupports2019Source 2needs review

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.
Claim 9capabilitysupports2019Source 2needs review

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.
Claim 10capabilitysupports2019Source 2needs review

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.
Claim 11capabilitysupports2019Source 2needs review

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.
Claim 12capabilitysupports2019Source 2needs review

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.
Claim 13comparative propertysupports2019Source 2needs review

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
Claim 14comparative propertysupports2019Source 2needs review

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
Claim 15comparative propertysupports2019Source 2needs review

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
Claim 16comparative propertysupports2019Source 2needs review

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
Claim 17comparative propertysupports2019Source 2needs review

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
Claim 18comparative propertysupports2019Source 2needs review

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
Claim 19comparative propertysupports2019Source 2needs review

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
Claim 20correlationsupports2019Source 2needs review

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...
Claim 21correlationsupports2019Source 2needs review

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...
Claim 22correlationsupports2019Source 2needs review

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...
Claim 23correlationsupports2019Source 2needs review

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...
Claim 24correlationsupports2019Source 2needs review

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...
Claim 25correlationsupports2019Source 2needs review

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...
Claim 26correlationsupports2019Source 2needs review

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...
Claim 27comparative performancesupports2018Source 3needs review

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.
Claim 28comparative performancesupports2018Source 3needs review

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.
Claim 29comparative performancesupports2018Source 3needs review

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.
Claim 30comparative performancesupports2018Source 3needs review

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.
Claim 31comparative performancesupports2018Source 3needs review

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.
Claim 32comparative performancesupports2018Source 3needs review

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.
Claim 33comparative performancesupports2018Source 3needs review

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.
Claim 34design rulesupports2018Source 3needs review

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.
Claim 35design rulesupports2018Source 3needs review

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.
Claim 36design rulesupports2018Source 3needs review

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.
Claim 37design rulesupports2018Source 3needs review

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.
Claim 38design rulesupports2018Source 3needs review

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.
Claim 39design rulesupports2018Source 3needs review

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.
Claim 40design rulesupports2018Source 3needs review

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.
Claim 41determinant of spatial confinementsupports2018Source 3needs review

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.
Claim 42determinant of spatial confinementsupports2018Source 3needs review

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.
Claim 43determinant of spatial confinementsupports2018Source 3needs review

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.
Claim 44determinant of spatial confinementsupports2018Source 3needs review

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.
Claim 45determinant of spatial confinementsupports2018Source 3needs review

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.
Claim 46determinant of spatial confinementsupports2018Source 3needs review

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.
Claim 47determinant of spatial confinementsupports2018Source 3needs review

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.
Claim 48tradeoffsupports2018Source 3needs review

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.
Claim 49tradeoffsupports2018Source 3needs review

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.
Claim 50tradeoffsupports2018Source 3needs review

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.
Claim 51tradeoffsupports2018Source 3needs review

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.
Claim 52tradeoffsupports2018Source 3needs review

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.
Claim 53tradeoffsupports2018Source 3needs review

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.
Claim 54tradeoffsupports2018Source 3needs review

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.
Claim 55application scopesupports2017Source 10needs review

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.
Claim 56tool optimizationsupports2017Source 10needs review

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.
Claim 57optimization reportsupports2016Source 4needs review

The paper reports optimized second-generation CRY2–CIB dimerizers.

Claim 58optimization reportsupports2016Source 4needs review

The paper reports optimized second-generation CRY2–CIB dimerizers.

Claim 59optimization reportsupports2016Source 4needs review

The paper reports optimized second-generation CRY2–CIB dimerizers.

Claim 60optimization reportsupports2016Source 4needs review

The paper reports optimized second-generation CRY2–CIB dimerizers.

Claim 61optimization reportsupports2016Source 4needs review

The paper reports optimized second-generation CRY2–CIB dimerizers.

Claim 62optimization reportsupports2016Source 4needs review

The paper reports optimized second-generation CRY2–CIB dimerizers.

Claim 63optimization reportsupports2016Source 4needs review

The paper reports optimized second-generation CRY2–CIB dimerizers.

Claim 64tool reportsupports2016Source 4needs review

The paper reports a photoactivatable Cre recombinase.

Claim 65tool reportsupports2016Source 4needs review

The paper reports a photoactivatable Cre recombinase.

Claim 66tool reportsupports2016Source 4needs review

The paper reports a photoactivatable Cre recombinase.

Claim 67tool reportsupports2016Source 4needs review

The paper reports a photoactivatable Cre recombinase.

Claim 68tool reportsupports2016Source 4needs review

The paper reports a photoactivatable Cre recombinase.

Claim 69tool reportsupports2016Source 4needs review

The paper reports a photoactivatable Cre recombinase.

Claim 70tool reportsupports2016Source 4needs review

The paper reports a photoactivatable Cre recombinase.

Claim 71assay applicationsupports2015Source 1needs review

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
Claim 72assay applicationsupports2015Source 1needs review

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
Claim 73assay applicationsupports2015Source 1needs review

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
Claim 74assay applicationsupports2015Source 1needs review

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
Claim 75assay applicationsupports2015Source 1needs review

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
Claim 76assay applicationsupports2015Source 1needs review

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
Claim 77assay applicationsupports2015Source 1needs review

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
Claim 78comparative characterizationsupports2015Source 1needs review

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
Claim 79comparative characterizationsupports2015Source 1needs review

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
Claim 80comparative characterizationsupports2015Source 1needs review

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
Claim 81comparative characterizationsupports2015Source 1needs review

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
Claim 82comparative characterizationsupports2015Source 1needs review

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
Claim 83comparative characterizationsupports2015Source 1needs review

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
Claim 84comparative characterizationsupports2015Source 1needs review

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
Claim 85correlationsupports2015Source 1needs review

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
Claim 86correlationsupports2015Source 1needs review

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
Claim 87correlationsupports2015Source 1needs review

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
Claim 88correlationsupports2015Source 1needs review

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
Claim 89correlationsupports2015Source 1needs review

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
Claim 90correlationsupports2015Source 1needs review

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
Claim 91correlationsupports2015Source 1needs review

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
Claim 92mechanistic effectsupports2015Source 1needs review

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.
Claim 93mechanistic effectsupports2015Source 1needs review

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.
Claim 94mechanistic effectsupports2015Source 1needs review

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.
Claim 95mechanistic effectsupports2015Source 1needs review

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.
Claim 96mechanistic effectsupports2015Source 1needs review

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.
Claim 97mechanistic effectsupports2015Source 1needs review

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.
Claim 98mechanistic effectsupports2015Source 1needs review

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.
Claim 99application demosupports2014Source 11needs review

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
Claim 100background activity comparisonsupports2014Source 11needs review

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
Claim 101benchmark resultsupports2014Source 11needs review

CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.

but similar responses between the CRY2/CIB and TULIP systems
Claim 102mechanism summarysupports2014Source 6needs review

Photoreceptor-based optogenetic tools in this review rely on light-dependent reversible binding to specific interaction partners.

Claim 103pathway regulation comparisonsupports2014Source 11needs review

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.

Source:

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

Source:

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...

Source:

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.

Source:

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.

Source:

optimization reportsupports

The paper reports optimized second-generation CRY2–CIB dimerizers.

Source:

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

Source:

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

Source:

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

Source:

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.

Source:

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.

Source:

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

Source:

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

Source:

benchmark resultsupports

CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.

but similar responses between the CRY2/CIB and TULIP systems

Source:

mechanism summarysupports

Photoreceptor-based optogenetic tools in this review rely on light-dependent reversible binding to specific interaction partners.

Source:

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

Source:

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.

Source:

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

Ranked Citations

  1. 1.
    StructuralSource 1ACS Synthetic Biology2015Claim 71Claim 72Claim 73

    Extracted from this source document.

  2. 2.
    StructuralSource 2Figshare2019Claim 6Claim 7Claim 8

    Extracted from this source document.

  3. 3.
    StructuralSource 3Proceedings of the National Academy of Sciences2018Claim 27Claim 28Claim 29

    Extracted from this source document.

  4. 4.
    StructuralSource 4Nature Chemical Biology2016Claim 57Claim 58Claim 59

    Seeded from load plan for claim c1. Extracted from this source document.

  5. 5.
    StructuralSource 5Journal of Experimental Neuroscience2017

    Extracted from this source document.

  6. 6.
    StructuralSource 6Biotechnology Journal2014Claim 102

    Extracted from this source document. Seeded from load plan for claim cl2.

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