Source 1primary paper2009The Plant Cell
Toolkit/CRY2-GFP
CRY2-GFP
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
CRY2-GFP is a C-terminal green fluorescent protein fusion of Arabidopsis cryptochrome 2 used to probe CRY2 blue-light responses. In the cited Plant Cell study, this fusion displayed constitutive biochemical and physiological activity and underwent blue-light-induced degradation more slowly than GFP-CRY2 or endogenous CRY2.
Usefulness & Problems
Why this is useful
This construct is useful as a comparative probe for how fusion orientation alters CRY2 signaling output and degradation behavior under blue light. It also provides a fluorescently tagged CRY2 variant for studying the relationship between CRY2 activity and light-dependent turnover, although the evidence provided does not detail imaging performance beyond the GFP fusion itself.
Source:
While GFP-CRY2 exerts light-dependent biochemical and physiological activities similar to those of the endogenous CRY2
Problem solved
CRY2-GFP helps address the construct-design problem of determining whether fluorescent tagging perturbs Arabidopsis CRY2 function and degradation. Specifically, it reveals that C-terminal GFP fusion can uncouple normal light dependence by producing constitutive activity and retarded blue-light-induced degradation.
Problem links
Need conditional protein clearance
DerivedCRY2-GFP is a C-terminal green fluorescent protein fusion of Arabidopsis cryptochrome 2 used to probe CRY2 blue-light responses. In the cited Plant Cell study, this fusion displayed constitutive biochemical and physiological activity and underwent blue-light-induced degradation more slowly than GFP-CRY2 or endogenous CRY2.
Need precise spatiotemporal control with light input
DerivedCRY2-GFP is a C-terminal green fluorescent protein fusion of Arabidopsis cryptochrome 2 used to probe CRY2 blue-light responses. In the cited Plant Cell study, this fusion displayed constitutive biochemical and physiological activity and underwent blue-light-induced degradation more slowly than GFP-CRY2 or endogenous CRY2.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Mechanisms
blue-light-dependent degradationconstitutive activationDegradationputative light-induced intramolecular domain disengagementTechniques
No technique tags yet.
Target processes
degradationInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: regulator
CRY2-GFP is implemented as a C-terminal GFP fusion to Arabidopsis CRY2, making fusion orientation a critical design variable. The available evidence supports use under blue-light stimulation and comparison against GFP-CRY2 or endogenous CRY2, but it does not provide details on expression system, promoter, cofactor requirements, or delivery method.
The cited evidence indicates that CRY2-GFP is constitutively active, so it does not faithfully reproduce the light-dependent behavior of endogenous CRY2. Validation appears limited to a single study and comparative observations, with no independent replication or broader performance data provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
CRY2-GFP shows constitutive biochemical and physiological activities.
CRY2-GFP showed constitutive biochemical and physiological activities
CRY2-GFP shows constitutive biochemical and physiological activities.
CRY2-GFP showed constitutive biochemical and physiological activities
CRY2-GFP shows constitutive biochemical and physiological activities.
CRY2-GFP showed constitutive biochemical and physiological activities
CRY2-GFP shows constitutive biochemical and physiological activities.
CRY2-GFP showed constitutive biochemical and physiological activities
CRY2-GFP shows constitutive biochemical and physiological activities.
CRY2-GFP showed constitutive biochemical and physiological activities
CRY2-GFP shows constitutive biochemical and physiological activities.
CRY2-GFP showed constitutive biochemical and physiological activities
CRY2-GFP shows constitutive biochemical and physiological activities.
CRY2-GFP showed constitutive biochemical and physiological activities
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
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
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
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
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
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
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
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
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
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
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
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
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
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
The nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded.
suggesting that the nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded
The nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded.
suggesting that the nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded
The nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded.
suggesting that the nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded
The nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded.
suggesting that the nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded
The nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded.
suggesting that the nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded
The nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded.
suggesting that the nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded
The nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded.
suggesting that the nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded
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.
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.
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.
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.
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.
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.
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.
CRY2-GFP is constitutively phosphorylated.
CRY2-GFP is constitutively phosphorylated
CRY2-GFP is constitutively phosphorylated.
CRY2-GFP is constitutively phosphorylated
CRY2-GFP is constitutively phosphorylated.
CRY2-GFP is constitutively phosphorylated
CRY2-GFP is constitutively phosphorylated.
CRY2-GFP is constitutively phosphorylated
CRY2-GFP is constitutively phosphorylated.
CRY2-GFP is constitutively phosphorylated
CRY2-GFP is constitutively phosphorylated.
CRY2-GFP is constitutively phosphorylated
CRY2-GFP is constitutively phosphorylated.
CRY2-GFP is constitutively phosphorylated
CRY2-GFP activates floral initiation in both long-day and short-day photoperiods.
it activates floral initiation in both long-day and short-day photoperiods
CRY2-GFP activates floral initiation in both long-day and short-day photoperiods.
it activates floral initiation in both long-day and short-day photoperiods
CRY2-GFP activates floral initiation in both long-day and short-day photoperiods.
it activates floral initiation in both long-day and short-day photoperiods
CRY2-GFP activates floral initiation in both long-day and short-day photoperiods.
it activates floral initiation in both long-day and short-day photoperiods
CRY2-GFP activates floral initiation in both long-day and short-day photoperiods.
it activates floral initiation in both long-day and short-day photoperiods
CRY2-GFP activates floral initiation in both long-day and short-day photoperiods.
it activates floral initiation in both long-day and short-day photoperiods
CRY2-GFP activates floral initiation in both long-day and short-day photoperiods.
it activates floral initiation in both long-day and short-day photoperiods
CRY2-GFP promotes deetiolation in both dark and light.
it promotes deetiolation in both dark and light
CRY2-GFP promotes deetiolation in both dark and light.
it promotes deetiolation in both dark and light
CRY2-GFP promotes deetiolation in both dark and light.
it promotes deetiolation in both dark and light
CRY2-GFP promotes deetiolation in both dark and light.
it promotes deetiolation in both dark and light
CRY2-GFP promotes deetiolation in both dark and light.
it promotes deetiolation in both dark and light
CRY2-GFP promotes deetiolation in both dark and light.
it promotes deetiolation in both dark and light
CRY2-GFP promotes deetiolation in both dark and light.
it promotes deetiolation in both dark and light
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
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
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
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
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
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
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
CRY2-GFP, but not GFP-CRY2, forms distinct nuclear bodies in response to blue light.
we found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light
CRY2-GFP, but not GFP-CRY2, forms distinct nuclear bodies in response to blue light.
we found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light
CRY2-GFP, but not GFP-CRY2, forms distinct nuclear bodies in response to blue light.
we found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light
CRY2-GFP, but not GFP-CRY2, forms distinct nuclear bodies in response to blue light.
we found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light
CRY2-GFP, but not GFP-CRY2, forms distinct nuclear bodies in response to blue light.
we found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light
CRY2-GFP, but not GFP-CRY2, forms distinct nuclear bodies in response to blue light.
we found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light
CRY2-GFP, but not GFP-CRY2, forms distinct nuclear bodies in response to blue light.
we found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light
Approval Evidence
1 source8 linked approval claimsfirst-pass slug cry2-gfp
CRY2-GFP
Source:
constitutive activitysupports
CRY2-GFP shows constitutive biochemical and physiological activities.
CRY2-GFP showed constitutive biochemical and physiological activities
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:
mechanistic interpretationsupports
The nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded.
suggesting that the nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded
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:
phosphorylation statesupports
CRY2-GFP is constitutively phosphorylated.
CRY2-GFP is constitutively phosphorylated
Source:
physiological activitysupports
CRY2-GFP activates floral initiation in both long-day and short-day photoperiods.
it activates floral initiation in both long-day and short-day photoperiods
Source:
physiological activitysupports
CRY2-GFP promotes deetiolation in both dark and light.
it promotes deetiolation in both dark and light
Source:
subcellular localization behaviorsupports
CRY2-GFP, but not GFP-CRY2, forms distinct nuclear bodies in response to blue light.
we found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light
Source:
Comparisons
Source-backed strengths
The construct was reported to retain measurable biochemical and physiological activity, indicating that the fusion protein is functionally active in the tested context. Its altered degradation kinetics relative to GFP-CRY2 and endogenous CRY2 make it informative for dissecting how tag placement affects CRY2 regulation.
Compared with GFP-CRY2
CRY2-GFP and GFP-CRY2 address a similar problem space because they share degradation.
Shared frame: same top-level item type; shared target processes: degradation; shared mechanisms: degradation; same primary input modality: light
Compared with lyso-ArchT
CRY2-GFP and lyso-ArchT address a similar problem space because they share degradation.
Shared frame: same top-level item type; shared target processes: degradation; shared mechanisms: degradation; same primary input modality: light
Compared with lyso-ChR2
CRY2-GFP and lyso-ChR2 address a similar problem space because they share degradation.
Shared frame: same top-level item type; shared target processes: degradation; shared mechanisms: degradation; same primary input modality: light
Ranked Citations
- 1.