Source 1primary paper2020UNC Libraries
Toolkit/Arabidopsis CRY2
Arabidopsis CRY2
Also known as: AtCRY2
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Arabidopsis cryptochrome 2 (AtCRY2) is a blue-light-responsive plant photoreceptor domain that has been heterologously expressed in mammalian cells. In that context, blue light induces AtCRY2 photobody formation and also triggers AtCRY2 degradation, providing a light-controlled module linked to protein clustering and turnover.
Usefulness & Problems
Why this is useful
AtCRY2 is useful as a light-input protein domain for imposing blue-light control over intracellular protein behavior in mammalian cells. The reported mammalian activity indicates that photobody formation does not require additional plant-specific proteins or nucleic acids beyond AtCRY2 itself, which supports its portability as an optogenetic component.
Source:
We found that light efficiently induces AtCRY2-PB formation in mammalian cells
Problem solved
AtCRY2 helps solve the problem of externally controlling protein organization and degradation with light in a heterologous mammalian setting. The cited work specifically supports its use for blue-light-induced photobody formation and light-responsive protein loss.
Problem links
Need conditional protein clearance
DerivedArabidopsis cryptochrome 2 (AtCRY2) is a blue-light-responsive plant photoreceptor that has been expressed in mammalian cells and shown to form photobodies under blue light. In this context, irradiation of AtCRY2 also leads to its degradation, providing a light-responsive protein domain linked to photobody formation and turnover.
Need precise spatiotemporal control with light input
DerivedArabidopsis cryptochrome 2 (AtCRY2) is a blue-light-responsive plant photoreceptor that has been expressed in mammalian cells and shown to form photobodies under blue light. In this context, irradiation of AtCRY2 also leads to its degradation, providing a light-responsive protein domain linked to photobody formation and turnover.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
Degradationlight-induced degradationlight-induced degradationlight-stimulated molecular association with mammalian cop1 e3 ligaselight-stimulated molecular association with mammalian cop1 e3 ligasephotobody formationphotobody formationTechniques
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: sensorswitch architecture: single chain
The available evidence indicates heterologous expression of AtCRY2 in mammalian cells as the implementation context. Blue light is the activating input, and no plant-specific proteins or nucleic acids beyond AtCRY2 itself were required for photobody formation in that setting.
The supplied evidence is limited to a small set of observations from a single study in mammalian cells. Quantitative performance parameters, wavelength-response details beyond blue light, kinetics, reversibility, and validation across multiple cell types or in vivo systems are not provided here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Irradiation of AtCRY2 leads to its degradation, and this degradation is not dependent on photobody formation.
Irradiation of AtCRY2 led to its degradation; however, degradation was not dependent upon photobody formation.
Blue light efficiently induces AtCRY2 photobody formation in mammalian cells.
We found that light efficiently induces AtCRY2-PB formation in mammalian cells
AtCRY2 photobody formation is associated with a light-stimulated interaction with mammalian COP1 E3 ligase.
AtCRY2 photobody formation is associated with light-stimulated interaction with mammalian COP1 E3 ligase
AtCRY2 photobody formation in mammalian cells does not require plant-specific proteins or nucleic acids beyond AtCRY2 itself.
indicating that, other than AtCRY2, no plant-specific proteins or nucleic acids are required for AtCRY2-PB formation
Approval Evidence
4 sources9 linked approval claimsfirst-pass slug arabidopsis-cry2
In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
Source:
we have expressed Arabidopsis CRY2 (AtCRY2) in mammalian cells
Source:
The Blue Light-Dependent Phosphorylation of the CCE Domain Determines the Photosensitivity of Arabidopsis CRY2
Source:
The Blue Light-Dependent Phosphorylation of the CCE Domain Determines the Photosensitivity of Arabidopsis CRY2
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mechanistic insightsupports
Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate distinct structural elements and critical residues that dynamically participate in photo-induced oligomerization.
Systematic structure-based analyses of photo-activated and inactive plant CRYs elucidate distinct structural elements and critical residues that dynamically partake in photo-induced oligomerization.
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mechanistic modelsupports
The study offers an updated model of cryptochrome photoactivation mechanism and its regulation by interacting proteins.
Our study offers an updated model of CRYs photoactivation mechanism as well as the mode of its regulation by interacting proteins.
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structural characterizationsupports
The study determined the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
In this study, we determine the crystal structure of the photosensory domain of Arabidopsis CRY2 in a tetrameric active state.
Source:
degradation behaviorsupports
Irradiation of AtCRY2 leads to its degradation, and this degradation is not dependent on photobody formation.
Irradiation of AtCRY2 led to its degradation; however, degradation was not dependent upon photobody formation.
Source:
functional activitysupports
Blue light efficiently induces AtCRY2 photobody formation in mammalian cells.
We found that light efficiently induces AtCRY2-PB formation in mammalian cells
Source:
molecular associationsupports
AtCRY2 photobody formation is associated with a light-stimulated interaction with mammalian COP1 E3 ligase.
AtCRY2 photobody formation is associated with light-stimulated interaction with mammalian COP1 E3 ligase
Source:
requirementsupports
AtCRY2 photobody formation in mammalian cells does not require plant-specific proteins or nucleic acids beyond AtCRY2 itself.
indicating that, other than AtCRY2, no plant-specific proteins or nucleic acids are required for AtCRY2-PB formation
Source:
functional determinantsupports
Blue light-dependent phosphorylation of the CCE domain determines the photosensitivity of Arabidopsis CRY2.
Source:
determinant relationshipsupports
Blue light-dependent phosphorylation of the CCE domain determines the photosensitivity of Arabidopsis CRY2.
The Blue Light-Dependent Phosphorylation of the CCE Domain Determines the Photosensitivity of Arabidopsis CRY2
Source:
Comparisons
Source-backed strengths
Blue light efficiently induces AtCRY2 photobody formation in mammalian cells, demonstrating robust responsiveness in a non-plant context. Photobody formation is associated with a light-stimulated interaction with mammalian COP1 E3 ligase, and degradation occurs upon irradiation even when it is not dependent on photobody formation.
Compared with blue light-inducible degradation (B-LID) domain
Arabidopsis CRY2 and blue light-inducible degradation (B-LID) domain 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
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with LOV2 domain-based optogenetic tool
Arabidopsis CRY2 and LOV2 domain-based optogenetic tool 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
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with photosensitive degron
Arabidopsis CRY2 and photosensitive degron 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
Strengths here: appears more independently replicated.
Ranked Citations
- 1.