Source 1primary paper2013ACS Synthetic Biology
Toolkit/Arabidopsis thaliana cryptochrome 2
Arabidopsis thaliana cryptochrome 2
Also known as: cryptochrome 2
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Arabidopsis thaliana cryptochrome 2 (CRY2) is a plant photoreceptor protein domain used as an optogenetic module. In the supplied evidence, CRY2 mediates blue light-dependent dimerization to activate C-RAF in mammalian cells.
Usefulness & Problems
Why this is useful
CRY2 is useful as a genetically encoded light-responsive domain for controlling signaling proteins with blue light. The supplied evidence specifically supports its use to optically induce C-RAF activation in mammalian cells through light-dependent dimerization.
Source:
Mediated by Arabidopsis thaliana photoreceptor cryptochrome 2, we activated the protein kinase C-RAF by blue light-dependent dimerization
Problem solved
This tool helps solve the problem of achieving reversible, externally triggered control of kinase signaling in mammalian cells. The evidence specifically indicates that it enables blue light-dependent activation of C-RAF.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
HeterodimerizationTechniques
No technique tags yet.
Target processes
signalingInput: Light
Implementation Constraints
The evidence indicates that CRY2 is derived from Arabidopsis thaliana and used in mammalian cells as part of an optogenetic construct. The current record supports domain fusion-based implementation for blue light-dependent control, but does not specify construct architecture, cofactors, expression conditions, or delivery method.
The supplied evidence is limited to a single claim about C-RAF activation in mammalian cells. It does not provide quantitative performance data, domain boundaries, kinetics, reversibility, spectral details beyond blue light, or broader validation across targets and systems.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
A cryptochrome 2-mediated optogenetic tool activates C-RAF by blue light-dependent dimerization in mammalian cells.
Mediated by Arabidopsis thaliana photoreceptor cryptochrome 2, we activated the protein kinase C-RAF by blue light-dependent dimerization
Approval Evidence
2 sources5 linked approval claimsfirst-pass slug arabidopsis-thaliana-cryptochrome-2
Mediated by Arabidopsis thaliana photoreceptor cryptochrome 2
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Arabidopsis thaliana cryptochrome 2 (CRY2)
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tool functionsupports
A cryptochrome 2-mediated optogenetic tool activates C-RAF by blue light-dependent dimerization in mammalian cells.
Mediated by Arabidopsis thaliana photoreceptor cryptochrome 2, we activated the protein kinase C-RAF by blue light-dependent dimerization
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degradation comparisonsupports
CRY2-GFP degradation is significantly retarded in response to blue light compared with GFP-CRY2 or endogenous CRY2.
Compared with GFP-CRY2 or the endogenous CRY2, CRY2-GFP degradation was significantly retarded in response to blue light
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functional activity comparisonsupports
GFP-CRY2 exhibits light-dependent biochemical and physiological activities similar to endogenous CRY2.
While GFP-CRY2 exerts light-dependent biochemical and physiological activities similar to those of the endogenous CRY2
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mechanistic interpretationsupports
The results are consistent with the hypothesis that photoexcited CRY2 disengages its C-terminal domain from the PHR domain to become active.
These results are consistent with the hypothesis that photoexcited CRY2 disengages its C-terminal domain from the PHR domain to become active.
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subcellular localization behaviorsupports
Both GFP-CRY2 and endogenous CRY2 form nuclear bodies in the presence of 26S-proteasome inhibitors that block blue light-dependent CRY2 degradation.
we showed that both GFP-CRY2 and endogenous CRY2 formed nuclear bodies in the presence of the 26S-proteasome inhibitors that block blue light-dependent CRY2 degradation
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Comparisons
Source-backed strengths
The evidence supports that CRY2 functions in mammalian cells despite being derived from Arabidopsis thaliana. Its key demonstrated advantage in the supplied material is blue light-dependent dimerization coupled to activation of a signaling kinase, C-RAF.
Ranked Citations
- 1.