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anti-Mouse (Murine) ARHGEF2 Antibodies:
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Human Monoclonal ARHGEF2 Primary Antibody for FACS, WB - ABIN2192013
Benais-Pont, Punn, Flores-Maldonado, Eckert, Raposo, Fleming, Cereijido, Balda, Matter: Identification of a tight junction-associated guanine nucleotide exchange factor that activates Rho and regulates paracellular permeability. in The Journal of cell biology 2003
Show all 4 Pubmed References
essential for neural tube closure
GEF-H1 was a novel regulator of inflammatory cytokine production and mycobacterial elimination, and may serve as a novel potential target for clinical treatment of tuberculosis.
Autophagic regulation of RhoA activity was dependent on GEF-H1 which directly bound to p62 and was degraded by autophagy, resulting in low RhoA activity. In contrast, the loss of autophagy increased GEF-H1 levels and thereby activated RhoA, which caused cells to move by amoeba-like migration. This amoeba-like migration was cancelled by the silencing of GEF-H1.
human brain malformation is recapitulated in Arhgef2 mutant mice and identify an aberrant migration of distinct components of the precerebellar system as a pathomechanism underlying the midbrain-hindbrain phenotype. Our results highlight the crucial function of ARHGEF2 in human brain development and identify a mutation in ARHGEF2 as novel cause of a neurodevelopmental disorder.
These results identify GEF-H1 as a component of the shear stress response machinery in neutrophils required for a fully competent immune response to bacterial infection.
Study describes a new mode of GEF-H1 activation in response to G-protein-coupled receptor (GPCR) ligands that is independent of microtubule depolymerization.
Data show that the activation of the microtubule-associated guanine nucleotide exchange factor GEF-H1, encoded by Arhgef2, is essential for sensing of foreign RNA by RIG-I-like receptors.
Pak2, but not Pak1, negatively regulates RhoA via phosphorylation of the guanine nucleotide exchange factor GEF-H1 at an inhibitory site, leading to increased GEF-H1 microtubule binding and loss of RhoA stimulation
It was shown that the guanine exchange factors GEF-H1 and ECT2 must be downregulated for megakaryote polyploidization. The first (2N-4N) endomitotic cycle requires GEF-H1 downregulation, whereas subsequent cycles (>4N) require ECT2 downregulation.
CAPN6 acts as a regulator of Rac1 and cell motility through interaction with GEF-H1.
LARG is activated by the Src family tyrosine kinase Fyn, whereas GEF-H1 catalytic activity is enhanced by ERK downstream of a signalling cascade that includes FAK and Ras
p114-RhoGEF and Lfc are critically involved in Wnt-3a- and Dvl-induced RhoA activation and neurite retraction in N1E-115 cells.
Depletion of GEF-H1 in the murine two-hit model of VILI attenuated vascular leak induced by lung ventilation at high tidal volume and thrombin-derived peptide TRAP6.
Enteropathogenic Escherichia coli type III effectors, EspG and its homolog Orf3, trigger the activation of the RhoA-ROCK signaling pathway via GEF-H1
PAK4 mediates morphological changes through regulation of GEF-H1
Microtubule-associated RhoGEF Lfc is required for the formation of the mitotic spindle during prophase/prometaphase.
Thus, Lfc and Tctex-1 interact to regulate cortical neurogenesis, potentially by regulating mitotic spindle orientation.
Authors identified a regulatory switch controlled by MARK3 that couples microtubules to the actin cytoskeleton to establish epithelial cell polarity through ARHGEF2.
depletion induces phosphorylation of the microtubule-associated GEF-H1 on Ser886, and thereby promotes RhoA activity and actin stress fiber assembly.
Overexpression of miR-194 downregulates the GEF-H1/RhoA pathway, inhibits melanoma cancer cell proliferation and metastasis. Furthermore, miR-194 expression is negatively associated with tumor-node-metastasis (TNM) stages
data suggest that the induction of SGK1 through treatment with dexamethasone alters MT dynamics to increase Sec5-GEF-H1 interactions, which promote GEF-H1 targeting to adhesion sites.
this study reports the crystal structure of human GEF-H1 PH domain to 2.45 A resolution.
By stimulating cofilin/PP2A-mediated dephosphorylation of the guanine nucleotide exchange factor GEF-H1.
regulation of c-Src trafficking requires both microtubules and actin polymerization, and GEF-H1 coordinates c-Src trafficking, acting as a molecular switch between these two mechanisms
Results supported that miR-512-3p could inhibit tumor cell adhesion, migration, and invasion by regulating the RAC1 activity via DOCK3 in NSCLC A549 and H1299 cell lines.
TGF-beta regulates LARG and GEF-H1 during epithelial-mesenchymal transition to affect stiffening response to force and cell invasion.
Our findings underscore a potent oncogenic role for GEF-H1 in promoting the metastatic potentials of hepatocellular carcinoma, possibly through activation of RhoA signalling.
Paxillin-GEF-H1-p42/44-MAPK module as a regulator of pathological mechanotransduction.
This study investigated a novel mechanism of vascular barrier protection by ANP via modulation of GEF-H1 function.
The RhoGEF GEF-H1 is required for oncogenic RAS signaling via KSR-1.
CAMSAP3-anchored non-centrosomal microtubules capture GEF-H1 more efficiently than other microtubules do.
ERK binds to the Rho exchange factor GEF-H1 and phosphorylates it on S959, causing inhibition of GEF-H1 activity and a consequent decrease in RhoA activity.
vincristine activates GEF-H1/RhoA/ROCK/MLC signaling.
extracellular matrix stiffness regulates RhoA through microtubule destabilization and the subsequent release and activation of GEF-H1.
present evidence that depletion of GEF-H1, a guanine nucleotide exchange factor for Rho proteins, affects vesicle trafficking
Data indicate that highly aggressive spindle-shaped 231BR3 cells changed to a round cell morphology associated with expression of the small GTPase guanine nucleotide exchange factor-H1 (GEF-H1).
Data indicate that TNF-alpha stimulates Rac, ADAM17/TACE, and RhoA through the guanine nucleotide exchange factor (GEF)-H1.
Data indicate that GEF-H1 is a target and functional effector of TGF-beta by orchestrating Rho signaling to regulate gene expression and cell migration.
ERK/GEF-H1/Rho/ROK/pMLC pathway could be a central mechanism whereby electrogenic transmembrane transport processes control myosin phosphorylation and regulate paracellular transport in the tubular epithelium.
the ERK/GEF-H1/Rho/Rho kinase/phospho-MLC pathway is the mechanism mediating TNF-alpha-induced elevation of tubular epithelial permeability, which in turn might contribute to kidney injury
Rho GTPases play a fundamental role in numerous cellular processes that are initiated by extracellular stimuli that work through G protein coupled receptors. The encoded protein may form complex with G proteins and stimulate rho-dependent signals. Alternatively spliced transcript variants encoding different isoforms have been identified.
Rho/Rac guanine nucleotide exchange factor (GEF) 2
, guanine nucleotide exchange factor LFC
, Rho/Rac guanine nucleotide exchange factor 2
, rho guanine nucleotide exchange factor 2-like
, LBC'S first cousin
, guanine nucleotide exchange factor H1
, lymphoid blast crisis-like 1
, oncogene LFC
, rho guanine nucleotide exchange factor 2
, microtubule-regulated Rho-GEF
, proliferating cell nucleolar antigen p40
, Guanine nucleotide exchange factor H1
, rho/rac guanine nucleotide exchange factor 2
, tight junction-associated guanine nucleotide exchange factor