Toolkit/BcLOV4-RhoA optogenetic fusion
BcLOV4-RhoA optogenetic fusion
Also known as: RhoA fused to BcLOV4
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The BcLOV4-RhoA optogenetic fusion is a single-transgene light-responsive construct in which RhoA GTPase, or its upstream activator ARHGEF11, is fused to BcLOV4. It enables spatiotemporally precise optical control of RhoA signaling and associated cytoskeletal and mechanotransductive responses without requiring a separate protein binding partner for dynamic membrane localization.
Usefulness & Problems
Why this is useful
This tool is useful for perturbing RhoA pathway activity with spatial and temporal precision using light. The cited study indicates that it supports control of downstream cytoskeletal morphology and mechanotransductive signaling while simplifying implementation through a single-transgene design.
Source:
permit spatiotemporally precise control over RhoA signaling
Source:
Direct membrane recruitment of these proteins induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Problem solved
It addresses the problem of inducing RhoA signaling with precise subcellular timing and localization while avoiding multi-component optogenetic systems that require protein binding partners for membrane recruitment. This is particularly relevant for experiments probing how localized RhoA activation shapes cell morphology and signaling outputs.
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 construct design consists of fusing BcLOV4 to either RhoA GTPase or the upstream activator ARHGEF11. The source establishes that the system is single-transgene and does not require protein binding partners for dynamic membrane localization, but the provided evidence does not detail expression systems, cofactors, or delivery modalities.
The available evidence indicates context dependence, because induced cytoskeletal morphology changes depend on alignment between spatially patterned stimulation and the underlying cell polarization. The provided evidence does not specify quantitative performance metrics, illumination wavelengths, kinetics, or validation across multiple cell types or organisms.
Validation
Supporting Sources
Ranked Claims
These single-transgene tools permit spatiotemporally precise control over RhoA signaling.
permit spatiotemporally precise control over RhoA signaling
These single-transgene tools permit spatiotemporally precise control over RhoA signaling.
permit spatiotemporally precise control over RhoA signaling
These single-transgene tools permit spatiotemporally precise control over RhoA signaling.
permit spatiotemporally precise control over RhoA signaling
These single-transgene tools permit spatiotemporally precise control over RhoA signaling.
permit spatiotemporally precise control over RhoA signaling
These single-transgene tools permit spatiotemporally precise control over RhoA signaling.
permit spatiotemporally precise control over RhoA signaling
These single-transgene tools permit spatiotemporally precise control over RhoA signaling.
permit spatiotemporally precise control over RhoA signaling
These single-transgene tools permit spatiotemporally precise control over RhoA signaling.
permit spatiotemporally precise control over RhoA signaling
Induced cytoskeletal morphology changes depend on the alignment of spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes are dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes depend on the alignment of spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes are dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes depend on the alignment of spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes are dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes depend on the alignment of spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes are dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes depend on the alignment of spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes are dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes depend on the alignment of spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes are dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes depend on the alignment of spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes are dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
These optogenetic tools are single-transgene tools that do not require protein binding partners for dynamic membrane localization.
These single-transgene tools do not require protein binding partners for dynamic membrane localization
These optogenetic tools are single-transgene tools that do not require protein binding partners for dynamic membrane localization.
These single-transgene tools do not require protein binding partners for dynamic membrane localization
These optogenetic tools are single-transgene tools that do not require protein binding partners for dynamic membrane localization.
These single-transgene tools do not require protein binding partners for dynamic membrane localization
These optogenetic tools are single-transgene tools that do not require protein binding partners for dynamic membrane localization.
These single-transgene tools do not require protein binding partners for dynamic membrane localization
These optogenetic tools are single-transgene tools that do not require protein binding partners for dynamic membrane localization.
These single-transgene tools do not require protein binding partners for dynamic membrane localization
These optogenetic tools are single-transgene tools that do not require protein binding partners for dynamic membrane localization.
These single-transgene tools do not require protein binding partners for dynamic membrane localization
These optogenetic tools are single-transgene tools that do not require protein binding partners for dynamic membrane localization.
These single-transgene tools do not require protein binding partners for dynamic membrane localization
RhoA-mediated cytoskeletal activation drives YAP nuclear localization within minutes and consequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation drives yes-associated protein (YAP) nuclear localization within minutes and consequent mechanotransduction verified by YAP-transcriptional enhanced associate domain transcriptional activity.
RhoA-mediated cytoskeletal activation drives YAP nuclear localization within minutes and consequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation drives yes-associated protein (YAP) nuclear localization within minutes and consequent mechanotransduction verified by YAP-transcriptional enhanced associate domain transcriptional activity.
RhoA-mediated cytoskeletal activation drives YAP nuclear localization within minutes and consequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation drives yes-associated protein (YAP) nuclear localization within minutes and consequent mechanotransduction verified by YAP-transcriptional enhanced associate domain transcriptional activity.
RhoA-mediated cytoskeletal activation drives YAP nuclear localization within minutes and consequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation drives yes-associated protein (YAP) nuclear localization within minutes and consequent mechanotransduction verified by YAP-transcriptional enhanced associate domain transcriptional activity.
RhoA-mediated cytoskeletal activation drives YAP nuclear localization within minutes and consequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation drives yes-associated protein (YAP) nuclear localization within minutes and consequent mechanotransduction verified by YAP-transcriptional enhanced associate domain transcriptional activity.
RhoA-mediated cytoskeletal activation drives YAP nuclear localization within minutes and consequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation drives yes-associated protein (YAP) nuclear localization within minutes and consequent mechanotransduction verified by YAP-transcriptional enhanced associate domain transcriptional activity.
RhoA-mediated cytoskeletal activation drives YAP nuclear localization within minutes and consequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation drives yes-associated protein (YAP) nuclear localization within minutes and consequent mechanotransduction verified by YAP-transcriptional enhanced associate domain transcriptional activity.
Direct membrane recruitment of BcLOV4-RhoA or BcLOV4-ARHGEF11 induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of these proteins induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of BcLOV4-RhoA or BcLOV4-ARHGEF11 induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of these proteins induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of BcLOV4-RhoA or BcLOV4-ARHGEF11 induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of these proteins induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of BcLOV4-RhoA or BcLOV4-ARHGEF11 induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of these proteins induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of BcLOV4-RhoA or BcLOV4-ARHGEF11 induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of these proteins induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of BcLOV4-RhoA or BcLOV4-ARHGEF11 induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of these proteins induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of BcLOV4-RhoA or BcLOV4-ARHGEF11 induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of these proteins induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
BcLOV4 can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet
Approval Evidence
RhoA GTPase, or its upstream activator ARHGEF11, is fused to BcLOV4
Source:
These single-transgene tools permit spatiotemporally precise control over RhoA signaling.
permit spatiotemporally precise control over RhoA signaling
Source:
Induced cytoskeletal morphology changes depend on the alignment of spatially patterned stimulation with the underlying cell polarization.
Induced cytoskeletal morphology changes are dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Source:
These optogenetic tools are single-transgene tools that do not require protein binding partners for dynamic membrane localization.
These single-transgene tools do not require protein binding partners for dynamic membrane localization
Source:
RhoA-mediated cytoskeletal activation drives YAP nuclear localization within minutes and consequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation drives yes-associated protein (YAP) nuclear localization within minutes and consequent mechanotransduction verified by YAP-transcriptional enhanced associate domain transcriptional activity.
Source:
Direct membrane recruitment of BcLOV4-RhoA or BcLOV4-ARHGEF11 induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Direct membrane recruitment of these proteins induces potent contractile signaling sufficient to separate adherens junctions with as little as one pulse of blue light.
Source:
Comparisons
Source-backed strengths
The reported strengths are single-transgene implementation, light-driven spatiotemporal control, and independence from auxiliary binding partners for dynamic membrane localization. The source also reports that patterned stimulation can induce cytoskeletal morphology changes, demonstrating functional coupling to downstream cellular responses.
Ranked Citations
- 1.