Source 1primary paper2021
Toolkit/single-component optogenetic tools for inducible RhoA GTPase signaling
single-component optogenetic tools for inducible RhoA GTPase signaling
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Single-component optogenetic tools were created to control RhoA GTPase signaling with light. The reported system does not require protein binding partners and enables inducible RhoA-mediated cytoskeletal activation with downstream YAP nuclear localization and YAP-TEAD mechanotranscription.
Usefulness & Problems
Why this is useful
These tools are useful for perturbing RhoA signaling with light while avoiding the need for separate binding-partner components. The reported outputs include cytoskeletal remodeling and rapid YAP-dependent mechanotransduction, making the system relevant for studying contractility-linked signaling.
Source:
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
Source:
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
Problem solved
The tool addresses the problem of optically inducing RhoA GTPase signaling in a single-component format rather than through multi-protein partner systems. It also provides a way to connect acute RhoA activation to downstream mechanotransduction readouts such as YAP nuclear localization and YAP-TEAD transcriptional activity.
Problem links
Need conditional control of signaling activity
DerivedSingle-component optogenetic tools were created to control RhoA GTPase signaling with light. The tools directly recruit fused effectors to the membrane without requiring protein binding partners, enabling inducible contractile signaling, cytoskeletal remodeling, and downstream YAP-dependent mechanotransduction.
Need conditional recombination or state switching
DerivedSingle-component optogenetic tools were created to control RhoA GTPase signaling with light. The tools directly recruit fused effectors to the membrane without requiring protein binding partners, enabling inducible contractile signaling, cytoskeletal remodeling, and downstream YAP-dependent mechanotransduction.
Need inducible protein relocalization or recruitment
DerivedSingle-component optogenetic tools were created to control RhoA GTPase signaling with light. The tools directly recruit fused effectors to the membrane without requiring protein binding partners, enabling inducible contractile signaling, cytoskeletal remodeling, and downstream YAP-dependent mechanotransduction.
Need precise spatiotemporal control with light input
DerivedSingle-component optogenetic tools were created to control RhoA GTPase signaling with light. The tools directly recruit fused effectors to the membrane without requiring protein binding partners, enabling inducible contractile signaling, cytoskeletal remodeling, and downstream YAP-dependent mechanotransduction.
Need tighter control over gene expression timing or amplitude
DerivedSingle-component optogenetic tools were created to control RhoA GTPase signaling with light. The tools directly recruit fused effectors to the membrane without requiring protein binding partners, enabling inducible contractile signaling, cytoskeletal remodeling, and downstream YAP-dependent mechanotransduction.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
Heterodimerizationlight-induced activation of rhoa signalinglight-induced activation of rhoa signalingmechanotransductionmechanotransductionmembrane recruitmentmembrane recruitmentMembrane RecruitmentTechniques
No technique tags yet.
Target processes
localizationrecombinationsignalingtranscriptionInput: 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 source supports that the system is a single-component optogenetic design for light control of RhoA GTPase signaling and that it does not require protein binding partners. However, the provided evidence does not describe cofactors, expression system, delivery method, membrane-targeting sequence, or exact fusion design.
The available evidence here is sparse and does not specify the photoreceptor module, wavelengths, construct architecture, or quantitative performance metrics. Reported cytoskeletal morphology changes were context dependent, because their outcome depended on alignment between spatially patterned stimulation and the underlying cell polarization.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
time to YAP nuclear localization within minutes
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
light pulse requirement as little as one pulse
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to 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 single-component-optogenetic-tools-for-inducible-rhoa-gtpase-signaling
We created optogenetic tools to control RhoA GTPase
Source:
context dependencesupports
Cytoskeletal morphology changes depended on the alignment of spatially patterned stimulation with the underlying cell polarization.
Cytoskeletal morphology changes were dependent on the alignment of the spatially patterned stimulation with the underlying cell polarization.
Source:
design propertysupports
These optogenetic tools are single-component and do not require protein binding partners.
These single-component tools, which do not require protein binding partners, offer spatiotemporally precise control over RhoA signaling
Source:
downstream signalingsupports
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction verified by YAP-TEAD transcriptional activity.
RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and subsequent mechanotransduction, verified by YAP- TEAD transcriptional activity.
Source:
functional effectsupports
Direct membrane recruitment of the fused effectors induced potent contractile signaling sufficient to separate adherens junctions after as little as one pulse of blue light.
Direct membrane recruitment of these effectors induced potent contractile signaling sufficient to separate adherens junctions in response to as little as one pulse of blue light.
Source:
tool mechanismsupports
RhoA GTPase or its upstream activating GEF effectors can be fused to BcLOV4 for light-regulated plasma membrane recruitment.
RhoA GTPase, or its upstream activating GEF effectors, were fused to BcLOV4, a photoreceptor that can be dynamically recruited to the plasma membrane by a light-regulated protein-lipid electrostatic interaction with the inner leaflet.
Source:
Comparisons
Source-backed strengths
A key strength is the single-component design, which the source states does not require protein binding partners. The literature also reports that RhoA-mediated cytoskeletal activation induced YAP nuclear localization within minutes and produced downstream YAP-TEAD transcriptional activity, supporting functional coupling from light input to mechanotransduction.
Compared with CRY2/CIB1
single-component optogenetic tools for inducible RhoA GTPase signaling and CRY2/CIB1 address a similar problem space because they share localization, recombination, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, recombination, signaling, transcription; shared mechanisms: heterodimerization; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
Compared with iLID/SspB
single-component optogenetic tools for inducible RhoA GTPase signaling and iLID/SspB address a similar problem space because they share localization, recombination, signaling, transcription.
Shared frame: same top-level item type; shared target processes: localization, recombination, 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
single-component optogenetic tools for inducible RhoA GTPase signaling 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.