Source 1primary paper2023eLife
Toolkit/TIAM1 GEF domain
TIAM1 GEF domain
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The TIAM1 GEF domain is a guanine-nucleotide exchange factor domain used as a modular component in Opto-RhoGEF systems. In the cited 2023 eLife study, Opto-RhoGEFs provided reversible light-responsive control of Rho GTPase-dependent endothelial morphology and vascular barrier strength.
Usefulness & Problems
Why this is useful
As a modular GEF domain within optogenetic Opto-RhoGEF constructs, the TIAM1 GEF domain supports precise control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction. The same system also enabled temporal control of vascular barrier strength in endothelial monolayers.
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
This domain helps address the need for reversible, optogenetic control of Rho GTPase signaling from global to subcellular scales in endothelial cells. The cited work specifically used Opto-RhoGEFs to control endothelial morphology and barrier strength with temporal precision.
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 TIAM1 GEF domain as a modular domain in domain-fused, light-responsive Opto-RhoGEF constructs. However, the supplied material does not report cofactor requirements, expression system details, delivery strategy, or specific fusion topology for the TIAM1-containing construct.
The supplied evidence identifies TIAM1 only as a source GEF domain used in Opto-RhoGEFs and does not provide domain-specific performance data separate from the broader Opto-RhoGEF system. The evidence also does not specify the exact photoreceptor architecture, activation wavelength, construct design details, or whether TIAM1-specific results were independently replicated.
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 tiam1-gef-domain
Guanine-nucleotide exchange factor (GEF) domains from ... TIAM1
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
The cited study reports precise optogenetic control over multiple endothelial morphological outputs, including size, roundness, local extension, and contraction. It also demonstrated 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.