Source 1primary paper2017Nature Communications
Toolkit/CRY2/CIBN light-gated dimerizer system
CRY2/CIBN light-gated dimerizer system
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The CRY2/CIBN light-gated dimerizer system is an optogenetic multi-component switch used to control subcellular RhoA activation through light-dependent recruitment of a CRY2-fused RhoA activator. In the cited implementation, the ARHGEF11 DHPH catalytic domain is fused to CRY2-mCherry to drive light-gated relocalization and thereby modulate force-related cellular phenotypes.
Usefulness & Problems
Why this is useful
This system is useful for manipulating cellular contractile forces with high spatiotemporal accuracy by controlling where RhoA is activated inside cells. In the reported study, light-directed recruitment enabled modulation of traction, intercellular tension, and tissue compaction through subcellular targeting of optoGEF-RhoA.
Source:
Here we report optogenetic tools to upregulate and downregulate such forces with high spatiotemporal accuracy.
Problem solved
It addresses the problem of perturbing RhoA signaling with precise spatial and temporal control rather than globally. The cited work specifically uses the system to control subcellular activation of RhoA and thereby tune force generation in different cellular compartments.
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
localizationsignalingtranscriptionInput: Light
Implementation Constraints
The reported construct design fuses the ARHGEF11 DHPH catalytic domain to CRY2-mCherry to create optoGEF-RhoA. Function depends on the CRY2/CIBN light-gated dimerizer system and subcellular targeting, with reported outcomes differing between plasma membrane recruitment and mitochondrial recruitment.
The supplied evidence is limited to one cited study and one implementation centered on RhoA control via an ARHGEF11 DHPH-CRY2-mCherry fusion. The evidence provided does not specify illumination wavelength, kinetic parameters, reversibility, dynamic range, or validation across multiple cell types or organisms.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The reported optogenetic tools can upregulate and downregulate cellular contractile forces with high spatiotemporal accuracy.
Here we report optogenetic tools to upregulate and downregulate such forces with high spatiotemporal accuracy.
The reported optogenetic tools can upregulate and downregulate cellular contractile forces with high spatiotemporal accuracy.
Here we report optogenetic tools to upregulate and downregulate such forces with high spatiotemporal accuracy.
The reported optogenetic tools can upregulate and downregulate cellular contractile forces with high spatiotemporal accuracy.
Here we report optogenetic tools to upregulate and downregulate such forces with high spatiotemporal accuracy.
The reported optogenetic tools can upregulate and downregulate cellular contractile forces with high spatiotemporal accuracy.
Here we report optogenetic tools to upregulate and downregulate such forces with high spatiotemporal accuracy.
The reported optogenetic tools can upregulate and downregulate cellular contractile forces with high spatiotemporal accuracy.
Here we report optogenetic tools to upregulate and downregulate such forces with high spatiotemporal accuracy.
The reported optogenetic tools can upregulate and downregulate cellular contractile forces with high spatiotemporal accuracy.
Here we report optogenetic tools to upregulate and downregulate such forces with high spatiotemporal accuracy.
The reported optogenetic tools can upregulate and downregulate cellular contractile forces with high spatiotemporal accuracy.
Here we report optogenetic tools to upregulate and downregulate such forces with high spatiotemporal accuracy.
optoGEF-RhoA is a fusion of the ARHGEF11 DHPH catalytic domain to CRY2-mCherry.
We fused the catalytic domain (DHPH domain) of the RhoA activator ARHGEF11 to CRY2-mCherry (optoGEF-RhoA)
optoGEF-RhoA is a fusion of the ARHGEF11 DHPH catalytic domain to CRY2-mCherry.
We fused the catalytic domain (DHPH domain) of the RhoA activator ARHGEF11 to CRY2-mCherry (optoGEF-RhoA)
optoGEF-RhoA is a fusion of the ARHGEF11 DHPH catalytic domain to CRY2-mCherry.
We fused the catalytic domain (DHPH domain) of the RhoA activator ARHGEF11 to CRY2-mCherry (optoGEF-RhoA)
optoGEF-RhoA is a fusion of the ARHGEF11 DHPH catalytic domain to CRY2-mCherry.
We fused the catalytic domain (DHPH domain) of the RhoA activator ARHGEF11 to CRY2-mCherry (optoGEF-RhoA)
optoGEF-RhoA is a fusion of the ARHGEF11 DHPH catalytic domain to CRY2-mCherry.
We fused the catalytic domain (DHPH domain) of the RhoA activator ARHGEF11 to CRY2-mCherry (optoGEF-RhoA)
optoGEF-RhoA is a fusion of the ARHGEF11 DHPH catalytic domain to CRY2-mCherry.
We fused the catalytic domain (DHPH domain) of the RhoA activator ARHGEF11 to CRY2-mCherry (optoGEF-RhoA)
optoGEF-RhoA is a fusion of the ARHGEF11 DHPH catalytic domain to CRY2-mCherry.
We fused the catalytic domain (DHPH domain) of the RhoA activator ARHGEF11 to CRY2-mCherry (optoGEF-RhoA)
Translocation of optoGEF-RhoA to mitochondria causes opposite changes in cellular traction, intercellular tension, and tissue compaction relative to plasma membrane translocation.
By contrast, translocation of optoGEF-RhoA to mitochondria results in opposite changes in these physical properties.
Translocation of optoGEF-RhoA to mitochondria causes opposite changes in cellular traction, intercellular tension, and tissue compaction relative to plasma membrane translocation.
By contrast, translocation of optoGEF-RhoA to mitochondria results in opposite changes in these physical properties.
Translocation of optoGEF-RhoA to mitochondria causes opposite changes in cellular traction, intercellular tension, and tissue compaction relative to plasma membrane translocation.
By contrast, translocation of optoGEF-RhoA to mitochondria results in opposite changes in these physical properties.
Translocation of optoGEF-RhoA to mitochondria causes opposite changes in cellular traction, intercellular tension, and tissue compaction relative to plasma membrane translocation.
By contrast, translocation of optoGEF-RhoA to mitochondria results in opposite changes in these physical properties.
Translocation of optoGEF-RhoA to mitochondria causes opposite changes in cellular traction, intercellular tension, and tissue compaction relative to plasma membrane translocation.
By contrast, translocation of optoGEF-RhoA to mitochondria results in opposite changes in these physical properties.
Translocation of optoGEF-RhoA to mitochondria causes opposite changes in cellular traction, intercellular tension, and tissue compaction relative to plasma membrane translocation.
By contrast, translocation of optoGEF-RhoA to mitochondria results in opposite changes in these physical properties.
Translocation of optoGEF-RhoA to mitochondria causes opposite changes in cellular traction, intercellular tension, and tissue compaction relative to plasma membrane translocation.
By contrast, translocation of optoGEF-RhoA to mitochondria results in opposite changes in these physical properties.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension, and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension, and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension, and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension, and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension, and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension, and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension, and tissue compaction.
Translocation of optoGEF-RhoA to the plasma membrane causes a rapid and local increase in cellular traction, intercellular tension and tissue compaction.
The technology controls subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology relies on controlling the subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology controls subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology relies on controlling the subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology controls subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology relies on controlling the subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology controls subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology relies on controlling the subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology controls subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology relies on controlling the subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology controls subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology relies on controlling the subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology controls subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology relies on controlling the subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
Changes in cellular contractility induced by the approach are paralleled by modifications in nuclear localization of YAP, indicating control of mechanotransductory signaling pathways in time and space.
Cellular changes in contractility are paralleled by modifications in the nuclear localization of the transcriptional regulator YAP, thus showing the ability of our approach to control mechanotransductory signalling pathways in time and space.
Changes in cellular contractility induced by the approach are paralleled by modifications in nuclear localization of YAP, indicating control of mechanotransductory signaling pathways in time and space.
Cellular changes in contractility are paralleled by modifications in the nuclear localization of the transcriptional regulator YAP, thus showing the ability of our approach to control mechanotransductory signalling pathways in time and space.
Changes in cellular contractility induced by the approach are paralleled by modifications in nuclear localization of YAP, indicating control of mechanotransductory signaling pathways in time and space.
Cellular changes in contractility are paralleled by modifications in the nuclear localization of the transcriptional regulator YAP, thus showing the ability of our approach to control mechanotransductory signalling pathways in time and space.
Changes in cellular contractility induced by the approach are paralleled by modifications in nuclear localization of YAP, indicating control of mechanotransductory signaling pathways in time and space.
Cellular changes in contractility are paralleled by modifications in the nuclear localization of the transcriptional regulator YAP, thus showing the ability of our approach to control mechanotransductory signalling pathways in time and space.
Changes in cellular contractility induced by the approach are paralleled by modifications in nuclear localization of YAP, indicating control of mechanotransductory signaling pathways in time and space.
Cellular changes in contractility are paralleled by modifications in the nuclear localization of the transcriptional regulator YAP, thus showing the ability of our approach to control mechanotransductory signalling pathways in time and space.
Changes in cellular contractility induced by the approach are paralleled by modifications in nuclear localization of YAP, indicating control of mechanotransductory signaling pathways in time and space.
Cellular changes in contractility are paralleled by modifications in the nuclear localization of the transcriptional regulator YAP, thus showing the ability of our approach to control mechanotransductory signalling pathways in time and space.
Changes in cellular contractility induced by the approach are paralleled by modifications in nuclear localization of YAP, indicating control of mechanotransductory signaling pathways in time and space.
Cellular changes in contractility are paralleled by modifications in the nuclear localization of the transcriptional regulator YAP, thus showing the ability of our approach to control mechanotransductory signalling pathways in time and space.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug cry2-cibn-light-gated-dimerizer-system
The technology relies on controlling the subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
Source:
capabilitysupports
The reported optogenetic tools can upregulate and downregulate cellular contractile forces with high spatiotemporal accuracy.
Here we report optogenetic tools to upregulate and downregulate such forces with high spatiotemporal accuracy.
Source:
mechanismsupports
The technology controls subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
The technology relies on controlling the subcellular activation of RhoA using the CRY2/CIBN light-gated dimerizer system.
Source:
signaling effectsupports
Changes in cellular contractility induced by the approach are paralleled by modifications in nuclear localization of YAP, indicating control of mechanotransductory signaling pathways in time and space.
Cellular changes in contractility are paralleled by modifications in the nuclear localization of the transcriptional regulator YAP, thus showing the ability of our approach to control mechanotransductory signalling pathways in time and space.
Source:
Comparisons
Source-backed strengths
The reported tools can upregulate and downregulate cellular contractile forces with high spatiotemporal accuracy. In the cited implementation, plasma membrane translocation of optoGEF-RhoA caused rapid and local increases in cellular traction, intercellular tension, and tissue compaction, while mitochondrial translocation produced opposite changes.
Ranked Citations
- 1.