Source 1primary paper2015ACS Synthetic Biology
Toolkit/CRY2-CRY2 interaction system
CRY2-CRY2 interaction system
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The CRY2-CRY2 interaction system is a blue-light-responsive optogenetic switch in which photoexcited cryptochrome 2 undergoes homo-oligomerization. In mammalian cells, this light-inducible interaction has been used to manipulate signaling pathways and cellular processes with high spatiotemporal precision.
Usefulness & Problems
Why this is useful
This system is useful for optogenetic control of protein behavior and cellular processes using light as a noninvasive input with high spatial and temporal precision. The cited study specifically positions CRY2 as a powerful and easy-to-apply tool in mammalian cells, and notes that membrane localization can strongly enhance oligomerization activity.
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 helps solve the problem of inducing reversible, light-dependent protein association inside mammalian cells to control localization-linked signaling and cellular responses. The evidence supports this through CRY2 light-inducible homo-oligomerization, particularly in contexts where stronger clustering is achieved at membranes.
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
localizationInput: Light
Implementation Constraints
The available evidence indicates that the system is implemented in mammalian cells and that membrane-bound CRY2 exhibits much stronger oligomerization than cytoplasmic CRY2. Construct localization is therefore an important design variable for tuning activity. No additional cofactor requirements, delivery methods, or domain truncation details are provided in the supplied evidence.
The supplied evidence is limited to a single 2015 source and does not provide quantitative kinetics, dynamic range, reversibility parameters, or wavelength details for the CRY2-CRY2 mode. Validation is described in mammalian cells, but broader organismal or in vivo performance is not documented here. Concomitant CRY2-CIB1 binding may complicate interpretation when both interaction modes are present in the same design.
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 source5 linked approval claimsfirst-pass slug cry2-cry2-interaction-system
the light-inducible CRY2-CRY2 and CRY2-CIB1 interaction systems
Source:
comparative activitysupports
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.
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
Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.
the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
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 CRY2 enables light-inducible manipulation of signaling pathways and cellular processes in mammalian cells with high spatiotemporal precision and ease of application. The reported oligomerization activity is drastically enhanced when CRY2 is membrane-bound relative to the cytoplasmic state, which can improve clustering-based responses. The system is also compatible with concomitant CRY2-CIB1 heterodimerization.
Source:
Quantitative analysis reveals that membrane-bound CRY2 has drastically enhanced oligomerization activity compared to that of its cytoplasmic form.
Ranked Citations
- 1.