Source 1primary paper2021Advanced Biology
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.
Problem links
Need conditional control of signaling activity
DerivedThe 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 downstream cytoskeletal and mechanotransductive responses.
Need inducible protein relocalization or recruitment
DerivedThe 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 downstream cytoskeletal and mechanotransductive responses.
Need precise spatiotemporal control with light input
DerivedThe 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 downstream cytoskeletal and mechanotransductive responses.
Need tighter control over gene expression timing or amplitude
DerivedThe 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 downstream cytoskeletal and mechanotransductive responses.
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
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment
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
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
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
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
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.
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.
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
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
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
time to YAP nuclear localization within minutes
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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.
light pulse requirement 1 pulse
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
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
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
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
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
1 source5 linked approval claimsfirst-pass slug bclov4-rhoa-optogenetic-fusion
RhoA GTPase, or its upstream activator ARHGEF11, is fused to BcLOV4
Source:
capabilitysupports
These single-transgene tools permit spatiotemporally precise control over RhoA signaling.
permit spatiotemporally precise control over RhoA signaling
Source:
context dependencesupports
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:
design propertysupports
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:
downstream signalingsupports
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:
functional effectsupports
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.
Compared with Cry2
BcLOV4-RhoA optogenetic fusion and Cry2 address a similar problem space because they share localization, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, signaling, transcription; shared mechanisms: heterodimerization, membrane recruitment, membrane_recruitment; same primary input modality: light
Strengths here: may avoid an exogenous cofactor requirement.
Relative tradeoffs: appears more independently replicated.
Compared with iLID/SspB
BcLOV4-RhoA optogenetic fusion and iLID/SspB address a similar problem space because they share localization, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, signaling, transcription; shared mechanisms: heterodimerization, membrane recruitment, membrane_recruitment; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with LOVpep/ePDZb
BcLOV4-RhoA optogenetic fusion and LOVpep/ePDZb address a similar problem space because they share localization, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, signaling, transcription; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
- 1.