Source 1primary paper2021Journal of Biological Chemistry
Toolkit/CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system
CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system
Also known as: Arabidopsis cryptochrome 2 fused to the N terminus of talin, dimerization module, N-terminal of cryptochrome-interacting basic helix-loop-helix domain ended with a CAAX box protein, optogenetic platform
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system is a blue-light-responsive two-component switch that fuses Arabidopsis cryptochrome 2 to the N terminus of full-length talin and anchors the N-terminal cryptochrome-interacting basic helix-loop-helix domain to the plasma membrane with a CAAX motif. In Chinese hamster ovary cells and endothelial cells, 450 nm illumination recruits talin to the plasma membrane and promotes activation of β3 integrins, including αIIbβ3- and αVβ3-associated complexes.
Usefulness & Problems
Why this is useful
This system enables acute optical control of talin localization at the plasma membrane, allowing direct testing of whether membrane recruitment of full-length talin is sufficient to drive integrin activation. It is useful for probing β3 integrin regulation and for manipulating endothelial cell migratory behavior with light.
Source:
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Source:
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Problem solved
The tool addresses the problem of causally linking talin plasma membrane localization to integrin activation in living cells. It provides a light-gated method to recruit talin without relying on constitutive targeting, enabling assessment of β3 integrin activation and downstream migration responses.
Problem links
Need conditional recombination or state switching
DerivedThe CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system is a blue-light-responsive, two-component switch in which Arabidopsis cryptochrome 2 is fused to the N terminus of full-length talin and the N-terminal cryptochrome-interacting basic helix-loop-helix domain is membrane-anchored with a CAAX motif. In Chinese hamster ovary cells and endothelial cells, 450 nm illumination recruits talin to the plasma membrane and promotes activation of β3 integrins, including αIIbβ3 and αVβ3-associated complexes.
Need inducible protein relocalization or recruitment
DerivedThe CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system is a blue-light-responsive, two-component switch in which Arabidopsis cryptochrome 2 is fused to the N terminus of full-length talin and the N-terminal cryptochrome-interacting basic helix-loop-helix domain is membrane-anchored with a CAAX motif. In Chinese hamster ovary cells and endothelial cells, 450 nm illumination recruits talin to the plasma membrane and promotes activation of β3 integrins, including αIIbβ3 and αVβ3-associated complexes.
Need precise spatiotemporal control with light input
DerivedThe CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system is a blue-light-responsive, two-component switch in which Arabidopsis cryptochrome 2 is fused to the N terminus of full-length talin and the N-terminal cryptochrome-interacting basic helix-loop-helix domain is membrane-anchored with a CAAX motif. In Chinese hamster ovary cells and endothelial cells, 450 nm illumination recruits talin to the plasma membrane and promotes activation of β3 integrins, including αIIbβ3 and αVβ3-associated complexes.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
HeterodimerizationHeterodimerizationlight-induced heterodimerizationlight-induced heterodimerizationmembrane recruitmentMembrane Recruitmentplasma membrane recruitmentplasma membrane recruitmentTechniques
No technique tags yet.
Target processes
localizationrecombinationInput: 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
The construct architecture consists of Arabidopsis CRY2 fused to the N terminus of full-length talin and a membrane-anchored CIBN component comprising the N-terminal cryptochrome-interacting basic helix-loop-helix domain terminated with a CAAX box. The system was inserted into Chinese hamster ovary cells and endothelial cells and activated with 450 nm blue light; no additional cofactors or delivery details are described in the supplied evidence.
The supplied evidence is limited to a single 2021 Journal of Biological Chemistry study and focuses on β3 integrin activation and endothelial migration. Quantitative performance characteristics, reversibility kinetics, background activity in the dark, and validation outside the reported cell contexts are not provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Approval Evidence
1 source2 linked approval claimsfirst-pass slug cry2-talin-cibn-caax-optogenetic-plasma-membrane-recruitment-system
Here, we used an optogenetic platform to assess whether recruitment of full-length talin to the plasma membrane was sufficient to induce integrin activation. A dimerization module (Arabidopsis cryptochrome 2 fused to the N terminus of talin; N-terminal of cryptochrome-interacting basic helix-loop-helix domain ended with a CAAX box protein [C: cysteine; A: aliphatic amino acid; X: any C-terminal amino acid]) responsive to 450 nm (blue) light was inserted into Chinese hamster ovary cells and endothelial cells
Source:
functional effectsupports
Blue-light-induced membrane recruitment of talin increases migration of endothelial cells.
This resulted in β3 integrin activation in both cell types, as well as increasing migration of the endothelial cells.
Source:
functional effectsupports
Blue-light-induced recruitment of CRY2-talin to the plasma membrane activates β3 integrins in Chinese hamster ovary cells and endothelial cells expressing αIIbβ3 or αVβ3.
Thus, exposure of the cells to blue light caused a rapid and reversible recruitment of Arabidopsis cryptochrome 2-talin to the ... plasma membrane. This resulted in β3 integrin activation in both cell types
Source:
Comparisons
Source-backed strengths
The reported system responds to 450 nm blue light and was validated in both Chinese hamster ovary cells and endothelial cells. Blue-light-induced recruitment of CRY2-talin to the plasma membrane activated β3 integrins in cells expressing αIIbβ3 or αVβ3, and membrane recruitment of talin increased endothelial cell migration.
Compared with Cry2/CIB
CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system and Cry2/CIB address a similar problem space because they share localization, recombination.
Shared frame: same top-level item type; shared target processes: localization, recombination; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with iLID/SspB
CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system and iLID/SspB address a similar problem space because they share localization, recombination.
Shared frame: same top-level item type; shared target processes: localization, recombination; shared mechanisms: heterodimerization, membrane_recruitment; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with SspB A58V iLID dimer variant
CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system and SspB A58V iLID dimer variant address a similar problem space because they share localization, recombination.
Shared frame: same top-level item type; shared target processes: localization, recombination; shared mechanisms: heterodimerization; same primary input modality: light
Ranked Citations
- 1.