Source 1primary paper2019Carolina Digital Repository (University of North Carolina at Chapel Hill)
Toolkit/Cry2-Cib photodimerizing pair
Cry2-Cib photodimerizing pair
Also known as: Cry2-Cib
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Cry2-Cib is a light-responsive photodimerizing protein pair used as a multi-component optogenetic switch. In the cited application, light stimulation drives translocation of a low-constitutive-activity protein kinase A catalytic subunit to a subcellular region containing Cib, thereby restoring kinase activity.
Usefulness & Problems
Why this is useful
This pair is useful for optogenetic control of signaling because light can recruit a fused effector protein to a defined subcellular region containing Cib. The supplied evidence specifically supports its use to restore protein kinase A activity through light-triggered relocalization.
Problem solved
It helps solve the problem of achieving light-dependent spatial control over kinase signaling. In the cited use case, it enables conditional activation of a low-constitutive-activity protein kinase A catalytic subunit by translocating it to a Cib-localized compartment.
Problem links
Need conditional control of signaling activity
DerivedCry2-Cib is a light-responsive photodimerizing protein pair used as a multi-component optogenetic switch. In the cited application, light stimulation drives translocation of a low-constitutive-activity protein kinase A catalytic subunit to a subcellular region containing Cib, thereby restoring kinase activity.
Need precise spatiotemporal control with light input
DerivedCry2-Cib is a light-responsive photodimerizing protein pair used as a multi-component optogenetic switch. In the cited application, light stimulation drives translocation of a low-constitutive-activity protein kinase A catalytic subunit to a subcellular region containing Cib, thereby restoring kinase activity.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
HeterodimerizationHeterodimerizationHeterodimerizationlight-induced protein translocationlight-induced protein translocationTechniques
No technique tags yet.
Target processes
signalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment
The cited implementation uses the Cry2-Cib pair with a low-constitutive-activity protein kinase A catalytic subunit whose activity is restored after light-induced translocation. Cib must be localized to the target subcellular region, implying construct design by protein fusion and localization engineering, but the evidence does not specify expression system, cofactors, or illumination parameters.
The supplied evidence is limited to a single described application and does not provide quantitative performance metrics, kinetics, wavelength details, reversibility, or dynamic range. Independent replication and broader validation across targets or organisms are not established by the provided material.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
Approval Evidence
1 source1 linked approval claimfirst-pass slug cry2-cib-photodimerizing-pair
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair.
Source:
mechanismsupports
The optogenetic protein kinase A uses the Cry2-Cib photodimerizing pair so that light stimulation translocates a low-constitutive-activity protein kinase A catalytic subunit to the subcellular region where Cib is localized and restores activity.
The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.
Source:
Comparisons
Source-backed strengths
The evidence supports that Cry2-Cib can couple light input to protein translocation and functional restoration of kinase activity. It also supports subcellularly localized control, because activity is restored specifically where Cib is localized.
Compared with fusion proteins with large N-terminal anchors
Cry2-Cib photodimerizing pair and fusion proteins with large N-terminal anchors address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Compared with LOVpep/ePDZb
Cry2-Cib photodimerizing pair and LOVpep/ePDZb address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with tandem-dimer nano (tdnano)
Cry2-Cib photodimerizing pair and tandem-dimer nano (tdnano) address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: heterodimerization; same primary input modality: light
Ranked Citations
- 1.FoundationalSource 1Carolina Digital Repository (University of North Carolina at Chapel Hill)2019Claim 1
Derived from 1 linked claims. Example evidence: The optogenetic protein kinase A takes advantage of the Cry2-Cib photodimerizing pair. In short, a protein kinase A catalytic subunit with low constitutive activity was fused to Cry2 such that, upon stimulation with light, it translocates to whatever subcellular region Cib is localized to and activity is restored.