Source 1primary paper2017
Toolkit/CRY2-mCherry-Drosophila β-catenin optogenetic switch
CRY2-mCherry-Drosophila β-catenin optogenetic switch
Also known as: Cryptochrome 2 (CRY2)-mCherry-Drosophila β-catenin fusion protein
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The CRY2-mCherry-Drosophila β-catenin optogenetic switch is a fusion protein comprising Arabidopsis thaliana CRY2, mCherry, and Drosophila β-catenin. Blue light induces oligomerization of the fusion protein, which inhibits downstream Wnt signaling in vitro and in vivo and enables temporal inactivation of β-catenin.
Usefulness & Problems
Why this is useful
This tool enables light-controlled perturbation of β-catenin/Wnt signaling with temporal precision in vitro and in vivo. The associated study further indicates that coupling this optogenetic switch with light-sheet microscopy supports precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Source:
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Problem solved
It addresses the need to acutely and reversibly inactivate β-catenin during development rather than relying only on static genetic perturbations. In the cited work, temporal inactivation was used to test when Wnt signaling is required for Drosophila pattern formation and later developmental maintenance.
Problem links
Need conditional control of signaling activity
DerivedThe CRY2-mCherry-Drosophila β-catenin optogenetic switch is a fusion protein comprising Arabidopsis thaliana CRY2, mCherry, and Drosophila β-catenin. Blue light induces oligomerization of the fusion protein, which inhibits downstream Wnt signaling in vitro and in vivo and enables temporal inactivation of β-catenin.
Need precise spatiotemporal control with light input
DerivedThe CRY2-mCherry-Drosophila β-catenin optogenetic switch is a fusion protein comprising Arabidopsis thaliana CRY2, mCherry, and Drosophila β-catenin. Blue light induces oligomerization of the fusion protein, which inhibits downstream Wnt signaling in vitro and in vivo and enables temporal inactivation of β-catenin.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
No technique tags yet.
Target processes
signalingInput: 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 component
The construct is formed by fusing Arabidopsis thaliana CRY2 to mCherry fluorescent protein and Drosophila β-catenin. Blue light is the stated input, and the cited work used the switch together with light-sheet microscopy for in vivo temporal perturbation studies.
The provided evidence is limited to a single 2017 source and does not report quantitative performance metrics such as activation wavelength range, kinetics, reversibility, dynamic range, or expression-dependent effects. Independent replication and validation outside the reported Drosophila/Wnt context are not documented in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Coupling optogenetics and light-sheet microscopy allows precise temporal regulation studies of signaling pathways and cellular processes in vivo.
Bringing the two approaches together allows unparalleled precision into the temporal regulation of signaling pathways and cellular processes in vivo .
Approval Evidence
1 source2 linked approval claimsfirst-pass slug cry2-mcherry-drosophila-catenin-optogenetic-switch
Cryptochrome 2 (CRY2) from Arabidopsis Thaliana was fused to mCherry fluorescent protein and Drosophila β–catenin to form an easy to visualize optogenetic switch.
Source:
biological conclusionsupports
Temporal inactivation of β-catenin confirmed that Wnt signaling is required for Drosophila pattern formation and for maintenance later in development.
Temporal inactivation of β–catenin confirmed that Wnt signaling is required not only for Drosophila pattern formation, but also for maintenance later in development.
Source:
mechanism of actionsupports
Blue light illumination causes oligomerization of the CRY2-mCherry-Drosophila β-catenin fusion protein and inhibits downstream Wnt signaling in vitro and in vivo.
Blue light illumination caused oligomerization of the fusion protein and inhibited downstream Wnt signaling in vitro and in vivo .
Source:
Comparisons
Source-backed strengths
The fusion is directly visualizable because it contains mCherry, and the reported response is triggered by blue light. The source reports inhibition of downstream Wnt signaling in both in vitro and in vivo settings, supporting utility across experimental contexts.
Compared with Cry2
CRY2-mCherry-Drosophila β-catenin optogenetic switch and Cry2 address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: oligomerization; same primary input modality: light
Strengths here: may avoid an exogenous cofactor requirement.
Relative tradeoffs: appears more independently replicated.
Compared with light-activated MLKL
CRY2-mCherry-Drosophila β-catenin optogenetic switch and light-activated MLKL address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: oligomerization; same primary input modality: light
Compared with optoRET
CRY2-mCherry-Drosophila β-catenin optogenetic switch and optoRET address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: oligomerization; same primary input modality: light
Ranked Citations
- 1.