Source 1primary paper2023eLife
Toolkit/p63RhoGEF GEF domain
p63RhoGEF GEF domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The p63RhoGEF GEF domain is a guanine-nucleotide exchange factor domain incorporated into Opto-RhoGEF constructs for light-controlled regulation of Rho GTPase signaling. In the cited 2023 eLife study, Opto-RhoGEFs using GEF domains including p63RhoGEF enabled reversible control of endothelial cell morphology and vascular endothelial barrier strength.
Usefulness & Problems
Why this is useful
This domain is useful as an effector module in optogenetic Rho-regulation systems that require spatially and temporally precise control of cell morphology and barrier-associated signaling. The cited study supports utility in endothelial cells for controlling cell size, roundness, local extension, contraction, and monolayer barrier strength.
Source:
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
Source:
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Source:
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
Source:
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
Problem solved
It helps solve the problem of reversibly controlling Rho GTPase signaling with light on global to subcellular scales. In the reported application, this enabled temporal control over endothelial morphological dynamics and vascular barrier regulation.
Source:
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
Source:
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
HeterodimerizationTechniques
No technique tags yet.
Target processes
localizationrecombinationsignalingInput: Light
Implementation Constraints
The available evidence supports use of the p63RhoGEF GEF domain as a fused component within Opto-RhoGEF constructs. The supplied material does not specify construct architecture, cofactors, expression system, or delivery method for the p63RhoGEF-containing implementation.
The supplied evidence identifies p63RhoGEF only as one source of a GEF domain and does not provide domain-specific performance data separated from other Opto-RhoGEF variants. No direct details are provided here on kinetics, dynamic range, spectral properties, or validation outside the cited endothelial-cell context.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.
Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.
This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.
found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin
The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
Approval Evidence
1 source1 linked approval claimfirst-pass slug p63rhogef-gef-domain
Guanine-nucleotide exchange factor (GEF) domains from ... p63RhoGEF
Source:
tool designsupports
GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.
Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).
Source:
Comparisons
Source-backed strengths
Evidence from the cited Opto-RhoGEF study indicates precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction. In endothelial monolayers, Opto-RhoGEFs also provided precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.
Source:
The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.
Ranked Citations
- 1.