Source 1primary paper2021Advanced Biology
Toolkit/BcLOV4-ARHGEF11 optogenetic fusion
BcLOV4-ARHGEF11 optogenetic fusion
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.
Problem links
Need conditional control of signaling activity
DerivedBcLOV4-ARHGEF11 optogenetic fusion is a single-transgene light-responsive construct in which the upstream RhoA activator ARHGEF11 is fused to BcLOV4. It enables inducible, spatiotemporally precise control of RhoA signaling through dynamic membrane localization without requiring a separate protein binding partner.
Need inducible protein relocalization or recruitment
DerivedBcLOV4-ARHGEF11 optogenetic fusion is a single-transgene light-responsive construct in which the upstream RhoA activator ARHGEF11 is fused to BcLOV4. It enables inducible, spatiotemporally precise control of RhoA signaling through dynamic membrane localization without requiring a separate protein binding partner.
Need precise spatiotemporal control with light input
DerivedBcLOV4-ARHGEF11 optogenetic fusion is a single-transgene light-responsive construct in which the upstream RhoA activator ARHGEF11 is fused to BcLOV4. It enables inducible, spatiotemporally precise control of RhoA signaling through dynamic membrane localization without requiring a separate protein binding partner.
Need tighter control over gene expression timing or amplitude
DerivedBcLOV4-ARHGEF11 optogenetic fusion is a single-transgene light-responsive construct in which the upstream RhoA activator ARHGEF11 is fused to BcLOV4. It enables inducible, spatiotemporally precise control of RhoA signaling through dynamic membrane localization without requiring a separate protein binding partner.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
Heterodimerizationlight-induced localization controllight-induced localization controlmembrane recruitmentmembrane recruitmentMembrane RecruitmentTechniques
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 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
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-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.
Compared with Cry2
BcLOV4-ARHGEF11 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-ARHGEF11 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-ARHGEF11 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.