Source 1primary paper2007Proceedings of the National Academy of Sciences
Toolkit/CRY2 C-terminal tail
CRY2 C-terminal tail
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The CRY2 C-terminal tail from Arabidopsis CRY2 contains an 80-residue NC80 motif that is sufficient to confer CRY2 physiological function. Evidence from transgenic plant studies indicates that this region participates in blue light-responsive regulation through phosphorylation-linked derepression of NC80.
Usefulness & Problems
Why this is useful
This domain is useful as a minimal light-regulated functional region for dissecting how Arabidopsis CRY2 is activated. The evidence suggests it can separate constitutive CRY2-like activity from blue light-induced phosphorylation, enabling mechanistic studies of cryptochrome regulation.
Source:
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
Problem solved
It helps address the problem of identifying which portion of the CRY2 C-terminal region is responsible for physiological output versus which portion is required for blue light-induced phosphorylation. The reported NC80 mapping defines a minimal functional motif within the larger C-terminal tail.
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
No target processes tagged yet.
Input: Light
Implementation Constraints
The evidence supports use of motif truncation within the Arabidopsis CRY2 C-terminal tail to isolate the 80-residue NC80 region. A GUS-NC80 fusion was expressed in transgenic plants, indicating that domain fusion and plant transgenic expression were used experimentally, but no additional construct or cofactor requirements are provided here.
The available evidence is limited to a single cited study in transgenic plants and focuses on physiological function and phosphorylation state. Quantitative performance, transferability to heterologous systems, and utility as a general optogenetic module are not established by the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug cry2-c-terminal-tail
the CRY2 C-terminal tail
Source:
requirement for phosphorylationsupports
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
Source:
structural modelsupports
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
Source:
Comparisons
Source-backed strengths
The strongest evidence is that the 80-residue NC80 motif was sufficient to confer CRY2 physiological function. In addition, a GUS-NC80 fusion expressed in transgenic plants was constitutively active but unphosphorylated, supporting functional separability between activity and phosphorylation.
Ranked Citations
- 1.