Toolkit Items

As a tool component, CIB1 is most directly supported as the cryptochrome-interacting bHLH partner used with CRY2 to create blue-light-controlled protein association systems. In these systems, CIB1 is typically fused to localization, transcriptional, or enzymatic modules so that blue light drives CRY2–CIB1 binding and light withdrawal reverses the interaction.

Enhanced Magnets (eMags) are Vivid-derived light-sensitive protein dimerization domains used in optogenetic split transcription factors and subcellular recruitment systems. In Saccharomyces cerevisiae, optimized eMag-based transcription factor designs improved light-sensitive gene expression, and eMags were also validated for rapid, reversible protein recruitment to subcellular organelles.

Light Activated BioID (LAB) is an optically controlled proximity-labeling system in which the two halves of split-TurboID are fused to the photodimerizing proteins CRY2 and CIB1. Blue light induces CRY2–CIB1 association, reconstituting split-TurboID and enabling proximity-dependent biotinylation of nearby proteins.

mOptoT7 is a mammalian optogenetic transcription system composed of a split T7 RNA polymerase fused to the blue-light-inducible nMag/pMag Magnets photodimerization system. Blue light drives reconstitution of the split polymerase to activate transcription from orthogonal T7 promoters in mammalian cells, and the system has been used to produce protein-coding mRNA, shRNA, and the Pepper RNA aptamer.

AAV-PA-Cre 3.0 is an adeno-associated viral delivery resource for the photoactivatable Cre recombinase 3.0 system, generated and validated for in vivo mouse applications. It delivers a blue-light-gated Cre/lox recombination system engineered for mammalian expression with reduced background recombination.

Cytoplasmically diffuse CRY2 with membrane-anchored CIBN is a proof-of-concept CRY2/CIB optogenetic configuration adapted into Drosophila-oriented vector systems. It was proposed to use blue light to recruit CRY2 fusion proteins, including a possible CRY2-Rho1 fusion, to the plasma membrane.

The CRY2-CIB1 optogenetic PIP3 production system is a blue-light-responsive multi-component switch built from Arabidopsis CRY2 and CIB1. It recruits a CRY2-fused constitutively active PI3-kinase from the cytosol to the plasma membrane through light-induced CRY2-CIB1 interaction, enabling sub-second spatiotemporal control of PIP3 production.

The iLID N414L variant is a modified iLID light-inducible dimerization system in which an N414L point mutation in the LOV domain lengthens the reversion half-life. In combination with SspB binding partners, it supports blue-light-dependent control of protein colocalization and has been used in reengineered iLID-SspB systems for processes including transmembrane protein localization.

The antiGFP nanobody is used as a targeting domain in an iLID fusion to localize the light-inducible iLID module to GFP-tagged proteins. In this configuration, blue-light illumination induces iLID-SspB heterodimerization while recruitment remains efficient at the GFP-labeled target.

The CIB1-TALE fusion targeting the Ascl1 promoter is a locus-anchoring component of a blue-light-responsive epigenetic editing system. In combination with CRY2 fused to the catalytic domain of DNMT3A or TET1, it enables light-induced recruitment at the Ascl1 promoter and modulation of promoter methylation state and gene activity.

Intracellular spatially segregated reporters of optoPAK1 activity are genetically designed reporter constructs intended to report optoPAK1-dependent phosphorylation at defined intracellular locations. The available evidence indicates that they were created alongside the light-responsive PAK1 analog optoPAK1 to monitor its activity after light-triggered relocalization.

This tool is a mathematical modeling method used together with an optogenetically engineered cell line and custom hardware to optically re-create calcium oscillation patterns. It enables independent variation of a single calcium waveform component within reconstructed oscillatory inputs.

iLID-nano is a multi-component optogenetic switch built from an improved light-induced dimerization pair comprising LOV2-SsrA and SspB. It has been used to control talin-mediated cell spreading and migration and has been physically characterized for force-coupled regulation in mechanotransduction contexts.

The CRY2-CIB1 receptor optogenetic activation system is a light-responsive multi-component switch based on the light-induced interaction between Cryptochrome 2 (CRY2) and CIB1. It was implemented as a bicistronic vector co-expressing CRY2 fused to the intracellular domain of a guidance receptor together with membrane-anchored CIB1, enabling local optical activation of receptor signaling in neurons.

The blue light-activated PKC isozyme recruitment system is a multi-component optogenetic switch that uses the plant-derived CRY2-CIB1 interaction to recruit PKC isozyme catalytic domains to the cell surface under blue light. In the reported format, CRY2-tagged PKC catalytic domains undergo light-triggered membrane translocation, and a PKCε implementation robustly activates GIRK1/4 potassium channels.

BphP1-Q-PAS1 is a near-infrared-light-inducible optogenetic interaction pair composed of BphP1 and Q-PAS1. It enables light-controlled protein regulation, including transcription-related applications and modification of chromatin epigenetic state, and it can be combined with blue-light LOV-domain systems with negligible spectral crosstalk.

CreLite is an optogenetically controlled Cre/loxP recombination system reported in developing zebrafish embryos. It uses split Cre recombinase halves fused to the red light-inducible partners PhyB and PIF6, so that 660 nm illumination in the presence of phycocyanobilin (PCB) restores Cre activity.

The CRY2 and LOV-fused degron light-responsive repression/degradation system is a multi-component optogenetic platform reported in mammalian cells that uses light to simultaneously block transcription and deplete protein levels. It is based on Arabidopsis cryptochrome 2 (CRY2), which interacts with CIB1 upon illumination, together with a LOV-fused degron configuration.

The CRY2-CIB1 interaction system is a blue-light-responsive optogenetic multi-component switch built from the light-inducible CRY2-CIB1 interaction system in mammalian cells. Photoexcited CRY2 supports inducible CRY2-CIB1 heterodimerization and can also undergo concomitant CRY2-CRY2 homo-oligomerization, enabling light-controlled manipulation of signaling pathways and cellular processes with high spatiotemporal precision.

The CRY2-CIB1 light-inducible transcription system is a multi-component optogenetic switch built from Arabidopsis cryptochrome 2 (CRY2) and CIB1 that drives protein expression by stimulating transcription in response to light. In mammalian cells, it uses light-triggered CRY2-CIB1 interaction to regulate gene expression and can also produce light-dependent redistribution of CRY2-tethered proteins within the nucleus.

The CRY2/CIBN light-gated dimerizer system is an optogenetic multi-component switch used to control subcellular RhoA activation through light-dependent recruitment of a CRY2-fused RhoA activator. In the cited implementation, the ARHGEF11 DHPH catalytic domain is fused to CRY2-mCherry to drive light-gated relocalization and thereby modulate force-related cellular phenotypes.

The CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system is a blue-light-responsive two-component switch that fuses Arabidopsis cryptochrome 2 to the N terminus of full-length talin and anchors the N-terminal cryptochrome-interacting basic helix-loop-helix domain to the plasma membrane with a CAAX motif. In Chinese hamster ovary cells and endothelial cells, 450 nm illumination recruits talin to the plasma membrane and promotes activation of β3 integrins, including αIIbβ3- and αVβ3-associated complexes.

The FKF1/GIGANTEA light-inducible transcription system is an optogenetic multi-component switch for mammalian cells built from the Arabidopsis photoreceptor FKF1 and its binding partner GIGANTEA. In an optimized split FKF1/GI dimerized Gal4-VP16 configuration, light induces transcriptional activation by reconstituting a functional transcriptional regulator.

iLID-antiGFP-nanobody is a multi-component optogenetic recruitment system in which iLID is fused to an antiGFP nanobody to target existing GFP-tagged proteins. Under blue-light illumination, iLID heterodimerizes with SspB, enabling light-dependent recruitment to locations defined by GFP fusions.

iLID-RTK is a blue-light-controlled, multi-component receptor tyrosine kinase switch built from the iLID and tdnano system. In darkness it is cytosolic, monomeric, and inactive, while blue light recruits two iLID-RTK molecules to tdnano to drive RTK dimerization and activation.

LADL (light-activated dynamic looping system) is a multi-component optogenetic genome-engineering platform that targets two genomic anchors with CRISPR guide RNAs and promotes their spatial co-localization through light-induced heterodimerization between CRY2 and dCas9-CIBN. In the cited 2018 study, this engineered looping altered endogenous gene expression, including increased nascent Zfp462 transcription and increased synchronous Sox2 expression.

PA-Cre2.0 is a photoactivatable split Cre recombinase in which Cre activity is reconstituted by light-induced CRY2-CIB1 dimerization. It enables light-dependent control of Cre-mediated recombination and has been functionally characterized in mammalian cells and rodent brain.

PhyB-CreC is the PhyB-fused C-terminal half of Cre recombinase in the CreLite optogenetic split-Cre system. In the presence of phycocyanobilin and 660 nm red light, it associates with PIF6-CreN to reconstitute Cre activity and drive Cre/loxP-dependent recombination in zebrafish embryos.

The Rho1-CRY2 fusion construct is a proposed optogenetic multi-component switch for Drosophila in which a small G protein Rho variant would be fused to CRY2. The intended function is blue-light-dependent recruitment of Rho1-CRY2 to membrane-anchored CIB to control subcellular localization and downstream events, but the available evidence indicates the construct was still being cloned rather than functionally validated.

The split synthetic zinc-finger transcription factor is a light-controlled transcriptional switch developed for Saccharomyces cerevisiae. Its activity is reconstituted from split components through CRY2- and CIB1-mediated light-induced dimerization, enabling optical control of gene expression.

The supplied web research summary states that the review spans photoactivatable genome editing and that the directly matching primary paper identifies the split Cas9 light-inducible system as paCas9 using pMag and nMag.

Here, we develop red/far-red light-regulated individually encapsulated (RL/FRL-EnE) cells, integrating optogenetics with biomaterial encapsulation for precise immunomodulation.

This system uses a phytochrome A-based photoswitch (ΔPhyA-PCB) that enables bidirectional control.