Source 1primary paper2015ACS Synthetic Biology
Toolkit/CRY2-CIB1 interaction system
CRY2-CIB1 interaction system
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The CRY2-CIB1 interaction system is a blue-light-responsive optogenetic multi-component switch built from the light-inducible CRY2-CIB1 interaction system in mammalian cells. Photoexcited CRY2 supports inducible CRY2-CIB1 heterodimerization and can also undergo concomitant CRY2-CRY2 homo-oligomerization, enabling light-controlled manipulation of signaling pathways and cellular processes with high spatiotemporal precision.
Usefulness & Problems
Why this is useful
This system is useful for optogenetic control of protein localization and pathway activity in mammalian cells using light as a noninvasive input with high spatiotemporal precision. The cited literature specifically describes it as powerful and easy to apply for light-inducible manipulation of signaling pathways and cellular processes.
Source:
The photoreceptor cryptochrome 2 (CRY2) has become a powerful optogenetic tool that allows light-inducible manipulation of various signaling pathways and cellular processes in mammalian cells with high spatiotemporal precision and ease of application.
Problem solved
It addresses the need for precise, reversible, light-gated control over intracellular interactions and localization-dependent cellular processes in mammalian cells. The evidence supports its use as a means to trigger defined CRY2-CIB1 interactions, while also accounting for concurrent CRY2 oligomerization behavior.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
Heterodimerizationlight-induced heterodimerizationlight-induced homo-oligomerizationOligomerizationTechniques
No technique tags yet.
Target processes
localizationInput: Light
Implementation Constraints
Implementation is based on a multi-component design using CRY2 and CIB1, consistent with domain-fusion-based optogenetic constructs. The evidence specifically notes that membrane-bound CRY2 exhibits much stronger oligomerization than cytoplasmic CRY2, so subcellular targeting is an important construct-design variable. The supplied evidence does not specify cofactors, delivery methods, or expression systems beyond use in mammalian cells.
The available evidence is limited to a single source and does not provide quantitative performance metrics such as kinetics, dynamic range, reversibility, or wavelength dependence beyond blue-light responsiveness in the tool description. Concurrent CRY2 homo-oligomerization may complicate interpretation or design when a purely heterodimeric response is desired, and membrane localization can strongly alter oligomerization behavior.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
CRY2 is a powerful optogenetic tool for light-inducible manipulation of signaling pathways and cellular processes in mammalian cells with high spatiotemporal precision and ease of application.
The photoreceptor cryptochrome 2 (CRY2) has become a powerful optogenetic tool that allows light-inducible manipulation of various signaling pathways and cellular processes in mammalian cells with high spatiotemporal precision and ease of application.
Membrane-bound CRY2 has drastically enhanced oligomerization activity compared with cytoplasmic CRY2.
Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.
Membrane-bound CRY2 has drastically enhanced oligomerization activity compared with cytoplasmic CRY2.
Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.
Membrane-bound CRY2 has drastically enhanced oligomerization activity compared with cytoplasmic CRY2.
Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.
Membrane-bound CRY2 has drastically enhanced oligomerization activity compared with cytoplasmic CRY2.
Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.
Membrane-bound CRY2 has drastically enhanced oligomerization activity compared with cytoplasmic CRY2.
Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.
Membrane-bound CRY2 has drastically enhanced oligomerization activity compared with cytoplasmic CRY2.
Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.
Membrane-bound CRY2 has drastically enhanced oligomerization activity compared with cytoplasmic CRY2.
Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.
CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.
While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.
While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.
While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.
While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.
While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.
While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.
While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Photoexcited CRY2 can undergo both homo-oligomerization and heterodimerization with CIB1 under blue light.
the photoexcited CRY2 can both undergo homo-oligomerization and heterodimerization by binding to its dimerization partner CIB1
Photoexcited CRY2 can undergo both homo-oligomerization and heterodimerization with CIB1 under blue light.
the photoexcited CRY2 can both undergo homo-oligomerization and heterodimerization by binding to its dimerization partner CIB1
Photoexcited CRY2 can undergo both homo-oligomerization and heterodimerization with CIB1 under blue light.
the photoexcited CRY2 can both undergo homo-oligomerization and heterodimerization by binding to its dimerization partner CIB1
Photoexcited CRY2 can undergo both homo-oligomerization and heterodimerization with CIB1 under blue light.
the photoexcited CRY2 can both undergo homo-oligomerization and heterodimerization by binding to its dimerization partner CIB1
Photoexcited CRY2 can undergo both homo-oligomerization and heterodimerization with CIB1 under blue light.
the photoexcited CRY2 can both undergo homo-oligomerization and heterodimerization by binding to its dimerization partner CIB1
Photoexcited CRY2 can undergo both homo-oligomerization and heterodimerization with CIB1 under blue light.
the photoexcited CRY2 can both undergo homo-oligomerization and heterodimerization by binding to its dimerization partner CIB1
Photoexcited CRY2 can undergo both homo-oligomerization and heterodimerization with CIB1 under blue light.
the photoexcited CRY2 can both undergo homo-oligomerization and heterodimerization by binding to its dimerization partner CIB1
Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.
the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.
the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.
the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.
the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.
the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.
the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.
the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Recruitment of cytoplasmic CRY2 to the membrane via interaction with membrane-bound CIB1 significantly intensifies CRY2 homo-oligomerization.
the homo-oligomerization of cytoplasmic CRY2 can be significantly intensified by its recruitment to the membrane via interaction with the membrane-bound CIB1
Recruitment of cytoplasmic CRY2 to the membrane via interaction with membrane-bound CIB1 significantly intensifies CRY2 homo-oligomerization.
the homo-oligomerization of cytoplasmic CRY2 can be significantly intensified by its recruitment to the membrane via interaction with the membrane-bound CIB1
Recruitment of cytoplasmic CRY2 to the membrane via interaction with membrane-bound CIB1 significantly intensifies CRY2 homo-oligomerization.
the homo-oligomerization of cytoplasmic CRY2 can be significantly intensified by its recruitment to the membrane via interaction with the membrane-bound CIB1
Recruitment of cytoplasmic CRY2 to the membrane via interaction with membrane-bound CIB1 significantly intensifies CRY2 homo-oligomerization.
the homo-oligomerization of cytoplasmic CRY2 can be significantly intensified by its recruitment to the membrane via interaction with the membrane-bound CIB1
Recruitment of cytoplasmic CRY2 to the membrane via interaction with membrane-bound CIB1 significantly intensifies CRY2 homo-oligomerization.
the homo-oligomerization of cytoplasmic CRY2 can be significantly intensified by its recruitment to the membrane via interaction with the membrane-bound CIB1
Recruitment of cytoplasmic CRY2 to the membrane via interaction with membrane-bound CIB1 significantly intensifies CRY2 homo-oligomerization.
the homo-oligomerization of cytoplasmic CRY2 can be significantly intensified by its recruitment to the membrane via interaction with the membrane-bound CIB1
Recruitment of cytoplasmic CRY2 to the membrane via interaction with membrane-bound CIB1 significantly intensifies CRY2 homo-oligomerization.
the homo-oligomerization of cytoplasmic CRY2 can be significantly intensified by its recruitment to the membrane via interaction with the membrane-bound CIB1
Approval Evidence
1 source3 linked approval claimsfirst-pass slug cry2-cib1-interaction-system
the light-inducible CRY2-CRY2 and CRY2-CIB1 interaction systems
Source:
interaction relationshipsupports
CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.
While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Source:
mechanismsupports
Photoexcited CRY2 can undergo both homo-oligomerization and heterodimerization with CIB1 under blue light.
the photoexcited CRY2 can both undergo homo-oligomerization and heterodimerization by binding to its dimerization partner CIB1
Source:
modulationsupports
Recruitment of cytoplasmic CRY2 to the membrane via interaction with membrane-bound CIB1 significantly intensifies CRY2 homo-oligomerization.
the homo-oligomerization of cytoplasmic CRY2 can be significantly intensified by its recruitment to the membrane via interaction with the membrane-bound CIB1
Source:
Comparisons
Source-backed strengths
A key strength is that the system enables light-inducible control in mammalian cells with high spatiotemporal precision and reported ease of application. The source also indicates that CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly, and that membrane-bound CRY2 shows drastically enhanced oligomerization activity relative to cytoplasmic CRY2.
Source:
Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.
Ranked Citations
- 1.