Toolkit/CRY2-CIB1 interaction system

CRY2-CIB1 interaction system

Multi-Component Switch·Research·Since 2015

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.

Problem links

Need inducible protein relocalization or recruitment

Derived

The CRY2-CIB1 interaction system is a blue-light-responsive optogenetic multi-component switch based on photoexcited CRY2, which heterodimerizes with CIB1 and can also undergo CRY2-CRY2 homo-oligomerization. In mammalian cells, it is used for light-inducible manipulation of signaling pathways and cellular processes with high spatiotemporal precision.

Need precise spatiotemporal control with light input

Derived

The CRY2-CIB1 interaction system is a blue-light-responsive optogenetic multi-component switch based on photoexcited CRY2, which heterodimerizes with CIB1 and can also undergo CRY2-CRY2 homo-oligomerization. In mammalian cells, it is used for light-inducible manipulation of signaling pathways and cellular processes with high spatiotemporal precision.

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

localization

Input: 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: actuatoroperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment

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

Claim 1capabilitysupports2015Source 1needs review

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.
Claim 2capabilitysupports2015Source 1needs review

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.
Claim 3capabilitysupports2015Source 1needs review

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.
Claim 4capabilitysupports2015Source 1needs review

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.
Claim 5capabilitysupports2015Source 1needs review

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.
Claim 6comparative activitysupports2015Source 1needs review

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.
Claim 7comparative activitysupports2015Source 1needs review

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.
Claim 8comparative activitysupports2015Source 1needs review

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.
Claim 9comparative activitysupports2015Source 1needs review

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.
Claim 10comparative activitysupports2015Source 1needs review

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.
Claim 11comparative activitysupports2015Source 1needs review

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.
Claim 12comparative activitysupports2015Source 1needs review

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.
Claim 13comparative activitysupports2015Source 1needs review

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.
Claim 14comparative activitysupports2015Source 1needs review

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.
Claim 15comparative activitysupports2015Source 1needs review

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.
Claim 16interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 17interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 18interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 19interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 20interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 21interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 22interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 23interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 24interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 25interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 26interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 27interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 28interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 29interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 30interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 31interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 32interaction relationshipsupports2015Source 1needs review

CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization can occur concomitantly.

While CRY2 homo-oligomerization and CRY2-CIB1 heterodimerization could happen concomitantly
Claim 33mechanismsupports2015Source 1needs review

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
Claim 34mechanismsupports2015Source 1needs review

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
Claim 35mechanismsupports2015Source 1needs review

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
Claim 36mechanismsupports2015Source 1needs review

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
Claim 37mechanismsupports2015Source 1needs review

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
Claim 38mechanismsupports2015Source 1needs review

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
Claim 39mechanismsupports2015Source 1needs review

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
Claim 40mechanismsupports2015Source 1needs review

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
Claim 41mechanismsupports2015Source 1needs review

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
Claim 42mechanismsupports2015Source 1needs review

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
Claim 43mechanismsupports2015Source 1needs review

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
Claim 44mechanismsupports2015Source 1needs review

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
Claim 45mechanismsupports2015Source 1needs review

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
Claim 46mechanismsupports2015Source 1needs review

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
Claim 47mechanismsupports2015Source 1needs review

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
Claim 48mechanismsupports2015Source 1needs review

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
Claim 49mechanismsupports2015Source 1needs review

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
Claim 50modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 51modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 52modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 53modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 54modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 55modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 56modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 57modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 58modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 59modulationsupports2015Source 1needs review

Certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization.

the presence of certain CIB1 fusion proteins can suppress CRY2 homo-oligomerization
Claim 60modulationsupports2015Source 1needs review

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
Claim 61modulationsupports2015Source 1needs review

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
Claim 62modulationsupports2015Source 1needs review

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
Claim 63modulationsupports2015Source 1needs review

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
Claim 64modulationsupports2015Source 1needs review

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
Claim 65modulationsupports2015Source 1needs review

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
Claim 66modulationsupports2015Source 1needs review

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
Claim 67modulationsupports2015Source 1needs review

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
Claim 68modulationsupports2015Source 1needs review

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
Claim 69modulationsupports2015Source 1needs review

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
Claim 70modulationsupports2015Source 1needs review

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
Claim 71modulationsupports2015Source 1needs review

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
Claim 72modulationsupports2015Source 1needs review

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
Claim 73modulationsupports2015Source 1needs review

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
Claim 74modulationsupports2015Source 1needs review

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
Claim 75modulationsupports2015Source 1needs review

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
Claim 76modulationsupports2015Source 1needs review

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.

CRY2-CIB1 interaction system and fusion proteins with large N-terminal anchors address a similar problem space because they share localization.

Shared frame: same top-level item type; shared target processes: localization; shared mechanisms: heterodimerization; same primary input modality: light

CRY2-CIB1 interaction system and light-inducible nuclear translocation and dimerization system address a similar problem space because they share localization.

Shared frame: same top-level item type; shared target processes: localization; shared mechanisms: heterodimerization; same primary input modality: light

Compared with LOVpep/ePDZb

CRY2-CIB1 interaction system and LOVpep/ePDZb address a similar problem space because they share localization.

Shared frame: same top-level item type; shared target processes: localization; shared mechanisms: heterodimerization; same primary input modality: light

Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.

Ranked Citations

  1. 1.
    StructuralSource 1ACS Synthetic Biology2015Claim 5Claim 5Claim 5

    Extracted from this source document.