Source 1primary paper2009The Plant Cell
Toolkit/GFP-CRY2
GFP-CRY2
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
GFP-CRY2 is an N-terminal green fluorescent protein fusion to Arabidopsis CRY2. In the cited Plant Cell study, this fusion retained blue light-dependent biochemical and physiological activities similar to endogenous CRY2 and showed blue light-responsive degradation behavior more similar to native CRY2 than the reciprocal CRY2-GFP construct.
Usefulness & Problems
Why this is useful
This construct is useful as a fluorescently tagged version of Arabidopsis CRY2 that preserves native-like blue light responsiveness better than a C-terminal GFP fusion. It addresses the need to visualize or track CRY2 while maintaining light-dependent activity and degradation properties associated with the endogenous photoreceptor.
Source:
While GFP-CRY2 exerts light-dependent biochemical and physiological activities similar to those of the endogenous CRY2
Problem solved
The specific problem addressed is how to fuse GFP to CRY2 without strongly perturbing CRY2 function. The cited evidence indicates that N-terminal GFP fusion avoids the constitutive activity and retarded blue light-induced degradation observed for CRY2-GFP.
Problem links
Need conditional protein clearance
DerivedGFP-CRY2 is an N-terminal green fluorescent protein fusion to Arabidopsis CRY2. In the cited Plant Cell study, this fusion retained blue light-dependent biochemical and physiological activities similar to endogenous CRY2 and showed blue light-responsive degradation behavior more similar to native CRY2 than the reciprocal CRY2-GFP construct.
Need precise spatiotemporal control with light input
DerivedGFP-CRY2 is an N-terminal green fluorescent protein fusion to Arabidopsis CRY2. In the cited Plant Cell study, this fusion retained blue light-dependent biochemical and physiological activities similar to endogenous CRY2 and showed blue light-responsive degradation behavior more similar to native CRY2 than the reciprocal CRY2-GFP construct.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Mechanisms
Degradationlight-dependent degradationlight-induced intramolecular conformational disengagement of the cry2 c-terminal domain from the phr domainTechniques
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
The construct design is an N-terminal GFP fusion to Arabidopsis CRY2. The relevant input modality is blue light, and the cited study specifically evaluated light-dependent biochemical, physiological, and degradation responses under blue light.
The evidence is limited to a comparative study against endogenous CRY2 and the reciprocal CRY2-GFP fusion in Arabidopsis CRY2 context. The supplied evidence does not provide quantitative performance metrics, broader cross-system validation, or direct mechanistic dissection for the GFP-CRY2 fusion itself beyond its light-dependent activity and degradation behavior.
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 source5 linked approval claimsfirst-pass slug gfp-cry2
GFP-CRY2
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:
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
GFP-CRY2 exhibited light-dependent biochemical and physiological activities similar to endogenous CRY2 in the reported study. Relative to CRY2-GFP, it also showed more native-like blue light-dependent degradation, supporting its use when preservation of endogenous CRY2 behavior is important.
Compared with lyso-ArchT
GFP-CRY2 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
GFP-CRY2 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
Compared with photo-caged PROTACs
GFP-CRY2 and photo-caged PROTACs 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.