Toolkit/Arabidopsis thaliana cryptochrome 2

Arabidopsis thaliana cryptochrome 2

Protein Domain·Research·Since 2013

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.

Problem links

Need conditional control of signaling activity

Derived

Arabidopsis thaliana cryptochrome 2 (CRY2) is a plant photoreceptor protein domain used in optogenetic systems. In the supplied evidence, it mediates blue light-dependent dimerization to activate C-RAF in mammalian cells.

Need precise spatiotemporal control with light input

Derived

Arabidopsis thaliana cryptochrome 2 (CRY2) is a plant photoreceptor protein domain used in optogenetic systems. In the supplied evidence, it mediates blue light-dependent dimerization to activate C-RAF in mammalian cells.

Taxonomy & Function

Primary hierarchy

Mechanism Branch

Component: A low-level protein part used inside a larger architecture that realizes a mechanism.

Techniques

No technique tags yet.

Target processes

signaling

Input: 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 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

Claim 1tool functionsupports2013Source 1needs review

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

Source:

Arabidopsis thaliana cryptochrome 2 (CRY2)

Source:

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

Source:

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

Source:

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

Source:

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.

Source:

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

Source:

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.

Compared with EL346

Arabidopsis thaliana cryptochrome 2 and EL346 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

Strengths here: appears more independently replicated; looks easier to implement in practice.

Compared with light-oxygen-voltage sensing (LOV) domain

Arabidopsis thaliana cryptochrome 2 and light-oxygen-voltage sensing (LOV) domain 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

Strengths here: appears more independently replicated; looks easier to implement in practice.

Compared with optogenetic RGS2

Arabidopsis thaliana cryptochrome 2 and optogenetic RGS2 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

Strengths here: appears more independently replicated; looks easier to implement in practice.

Ranked Citations

  1. 1.
    FoundationalSource 1ACS Synthetic Biology2013Claim 1

    Derived from 1 linked claims. Example evidence: Mediated by Arabidopsis thaliana photoreceptor cryptochrome 2, we activated the protein kinase C-RAF by blue light-dependent dimerization