Toolkit/BcLOV4-ARHGEF11 optogenetic fusion

BcLOV4-ARHGEF11 optogenetic fusion

Multi-Component Switch·Research·Since 2021

Also known as: ARHGEF11 fused to BcLOV4

Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.

Summary

BcLOV4-ARHGEF11 is a single-transgene optogenetic fusion in which the upstream RhoA activator ARHGEF11 is fused to BcLOV4. It enables light-inducible, spatiotemporally precise control of RhoA signaling through dynamic membrane localization without requiring a separate protein binding partner.

Usefulness & Problems

Why this is useful

This tool is useful for perturbing RhoA pathway activity with spatial and temporal precision using a single genetic construct. The cited study indicates that it supports control of signaling and associated cytoskeletal morphology changes while avoiding the need for an additional binding partner for membrane recruitment.

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 achieving inducible RhoA signaling control with dynamic membrane localization using a simpler single-transgene architecture. The source specifically frames these tools as avoiding dependence on separate protein binding partners while permitting precise optical control.

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

localizationsignalingtranscription

Input: Light

Implementation Constraints

The construct design consists of ARHGEF11 fused to BcLOV4 as a single transgene. The supplied evidence supports light-responsive dynamic membrane localization, but it does not provide further practical details such as linker design, expression system, cofactor requirements, or delivery modality.

The reported response is context dependent, because induced cytoskeletal morphology changes depend on how patterned stimulation aligns with pre-existing cell polarization. The provided evidence does not specify quantitative performance, illumination wavelength, kinetics, or validation across multiple model systems.

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1capabilitysupports2021Source 1needs review

These single-transgene tools permit spatiotemporally precise control over RhoA signaling.

permit spatiotemporally precise control over RhoA signaling
Claim 2capabilitysupports2021Source 1needs review

These single-transgene tools permit spatiotemporally precise control over RhoA signaling.

permit spatiotemporally precise control over RhoA signaling
Claim 3capabilitysupports2021Source 1needs review

These single-transgene tools permit spatiotemporally precise control over RhoA signaling.

permit spatiotemporally precise control over RhoA signaling
Claim 4capabilitysupports2021Source 1needs review

These single-transgene tools permit spatiotemporally precise control over RhoA signaling.

permit spatiotemporally precise control over RhoA signaling
Claim 5capabilitysupports2021Source 1needs review

These single-transgene tools permit spatiotemporally precise control over RhoA signaling.

permit spatiotemporally precise control over RhoA signaling
Claim 6capabilitysupports2021Source 1needs review

These single-transgene tools permit spatiotemporally precise control over RhoA signaling.

permit spatiotemporally precise control over RhoA signaling
Claim 7capabilitysupports2021Source 1needs review

These single-transgene tools permit spatiotemporally precise control over RhoA signaling.

permit spatiotemporally precise control over RhoA signaling
Claim 8context dependencesupports2021Source 1needs review

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.
Claim 9context dependencesupports2021Source 1needs review

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.
Claim 10context dependencesupports2021Source 1needs review

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.
Claim 11context dependencesupports2021Source 1needs review

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.
Claim 12context dependencesupports2021Source 1needs review

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.
Claim 13context dependencesupports2021Source 1needs review

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.
Claim 14context dependencesupports2021Source 1needs review

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.
Claim 15design propertysupports2021Source 1needs review

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
Claim 16design propertysupports2021Source 1needs review

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
Claim 17design propertysupports2021Source 1needs review

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
Claim 18design propertysupports2021Source 1needs review

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
Claim 19design propertysupports2021Source 1needs review

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
Claim 20design propertysupports2021Source 1needs review

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
Claim 21design propertysupports2021Source 1needs review

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
Claim 22downstream signalingsupports2021Source 1needs review

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
Claim 23downstream signalingsupports2021Source 1needs review

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
Claim 24downstream signalingsupports2021Source 1needs review

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
Claim 25downstream signalingsupports2021Source 1needs review

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
Claim 26downstream signalingsupports2021Source 1needs review

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
Claim 27downstream signalingsupports2021Source 1needs review

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
Claim 28downstream signalingsupports2021Source 1needs review

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
Claim 29functional effectsupports2021Source 1needs review

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
Claim 30functional effectsupports2021Source 1needs review

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
Claim 31functional effectsupports2021Source 1needs review

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
Claim 32functional effectsupports2021Source 1needs review

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
Claim 33functional effectsupports2021Source 1needs review

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
Claim 34functional effectsupports2021Source 1needs review

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
Claim 35functional effectsupports2021Source 1needs review

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
Claim 36mechanismsupports2021Source 1needs review

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-arhgef11-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

Reported strengths are single-component design, spatiotemporal precision, and dynamic membrane localization. The literature also indicates that induced cytoskeletal morphology changes can be spatially patterned, although their outcome depends on alignment with the cell’s underlying polarization.

Ranked Citations

  1. 1.
    StructuralSource 1Advanced Biology2021Claim 1Claim 2Claim 3

    Extracted from this source document.