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Vav 2 guanine nucleotide exchange factor

VAV2 is the second member of the VAV guanine nucleotide exchange factor family of oncogenes. Unlike VAV1, which is expressed exclusively in hematopoietic cells, VAV2 transcripts were found in most tissues. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2008] (from NCBI)
Top mentioned proteins: NBS1, Rhodopsin, Rac1, CAN, Vav3
Papers using Vav2 antibodies
Vav2 is required for cell spreading
Carpenter Christopher L. et al., In The Journal of Cell Biology, 1994
... Mutations in the DH and PH domains were generated in T7 epitope–tagged Vav2 in pCMV5 using the Transformer site–directed mutagenesis kit (CLONTECH Laboratories, Inc.) ...
Papers on Vav2
VAV2, a guanine nucleotide exchange factor for Rac1, regulates glucose-stimulated insulin secretion in pancreatic beta cells.
Kowluru et al., Detroit, United States. In Diabetologia, Nov 2015
Guanine nucleotide exchange factor VAV2 (VAV2), a member of the Dbl family of proteins, has been identified as one of the GDP/GTP exchange factors for Rac1.
Differential Gene Expression of the Proto-oncogene VAV3 and the Transcript Variant VAV3.1 in Oral Squamous Cell Carcinoma.
Sieg et al., Lübeck, Germany. In Anticancer Res, May 2015
The VAV proteins VAV1, VAV2 and VAV3 have been identified as important molecules in tumorigenesis, tumor growth and cell migration.
Vimentin regulates lung cancer cell adhesion through a VAV2-Rac1 pathway to control focal adhesion kinase activity.
Marcus et al., Atlanta, United States. In Oncogene, May 2015
We identified the guanine nucleotide exchange factor (GEF), VAV2, as having the greatest loss of phosphorylation owing to vimentin depletion.
The P2Y2 Receptor Interacts with VE-Cadherin and VEGF Receptor-2 to Regulate Rac1 Activity in Endothelial Cells.
Erb et al., San Diego, United States. In J Biomed Sci Eng, 2015
Activation of the P2Y2R by UTP also caused a prolonged interaction between p120 catenin and vav2 (a guanine nucleotide exchange factor for Rac) that correlated with the kinetics of UTP-induced tyrosine phosphorylation of p120 catenin and VE-cadherin.
Genetic dissection of the vav2-rac1 signaling axis in vascular smooth muscle cells.
Bustelo et al., Salamanca, Spain. In Mol Cell Biol, 2014
Here, we show that the expression of an active version of the Rac1 activator Vav2 exclusively in vSMCs leads to hypotension as well as the elimination of the hypertension induced by the systemic loss of wild-type Vav2.
Genome-wide whole blood microRNAome and transcriptome analyses reveal miRNA-mRNA regulated host response to foodborne pathogen Salmonella infection in swine.
Guan et al., Edmonton, Canada. In Sci Rep, 2014
An miRNA seed sequence analysis suggested that these miRNAs regulate several critical immune-related genes including SLC11A1, PIGE-108A11.3 and VAV2.
Identification of melanoma biomarkers based on network modules by integrating the human signaling network with microarrays.
Chen et al., Shanghai, China. In J Cancer Res Ther, 2014
Finally, we acquired six significant molecular biomarkers, namely, module 10 (CALM3, Ca 2+ , PKC, PDGFRA, phospholipase-g, PIB5PA, and phosphatidylinositol-3-kinase), module 14 (SRC, Src homology 2 domain-containing [SHC], SAM68, GIT1, transcription factor-4, CBLB, GRB2, VAV2, LCK, YES, PTCH2, downstream of tyrosine kinase [DOK], and KIT), module 16 (ELK3, p85beta, SHC, ZFYVE9, TGFBR1, TGFBR2, CITED1, SH3KBP1, HCK, DOK, and KIT), module 45 (RB, CCND3, CCNA2, CDK4, and CDK6), module 75 (PCNA, CDK4, and CCND1), and module 114 (PSD93, NMDAR, and FYN).
Silencing of miRNA-148a by hypermethylation activates the integrin-mediated signaling pathway in nasopharyngeal carcinoma.
Chang et al., Anyang, China. In Oncotarget, 2014
The ectopic expression of miR-148a inhibits cell migration in NPC cells through the suppression of integrin-mediated signaling by targeting VAV2, WASL and ROCK1.
PTP-PEST targets a novel tyrosine site in p120 catenin to control epithelial cell motility and Rho GTPase activity.
Sastry et al., Galveston, United States. In J Cell Sci, 2014
Furthermore, p120 localization is enhanced at actin-rich protrusions and lamellipodia and has an increased association with the guanine nucleotide exchange factor, VAV2, and cortactin.
MicroRNA-195 suppresses angiogenesis and metastasis of hepatocellular carcinoma by inhibiting the expression of VEGF, VAV2, and CDC42.
Zhuang et al., Guangzhou, China. In Hepatology, 2013
Subsequent investigations disclosed that miR-195 directly inhibited the expression of the proangiogenic factor vascular endothelial growth factor (VEGF) and the prometastatic factors VAV2 and CDC42.
Molecular genetic analysis of primary open-angle glaucoma, normal tension glaucoma, and developmental glaucoma for the VAV2 and VAV3 gene variants in Japanese subjects.
Fuse et al., Shenyang, China. In Biochem Biophys Res Commun, 2013
We studied 168 unrelated Japanese patients with primary open-angle glaucoma (POAG), 163 unrelated Japanese patients with normal tension glaucoma (NTG), 45 unrelated Japanese patients with developmental glaucoma (DG), and 180 ethnically matched normal controls, to determine whether variants in the vav 2 guanine nucleotide exchange factor (VAV2) and vav 3 guanine nucleotide exchange factor (VAV3) genes are associated with POAG, NTG, or DG in the Japanese.
Dissecting GRB7-mediated signals for proliferation and migration in HER2 overexpressing breast tumor cells: GTP-ase rules.
Leyland-Jones et al., Sioux Falls, United States. In Am J Cancer Res, 2012
This FAK-GRB7 complex leads to downstream activation of RAC1-GTP (responsible for migration) probably through the recruitment of VAV2.
The rho exchange factors vav2 and vav3 control a lung metastasis-specific transcriptional program in breast cancer cells.
Bustelo et al., Salamanca, Spain. In Sci Signal, 2012
We report that two Rho GEFs, Vav2 and Vav3, play synergistic roles in breast cancer by sustaining tumor growth, neoangiogenesis, and many of the steps involved in lung-specific metastasis.
The guanine nucleotide exchange factor Vav2 is a negative regulator of parathyroid hormone receptor/Gq signaling.
Klenk et al., Würzburg, Germany. In Mol Pharmacol, 2012
VAV2 specifically interacts with activated Galpha(q) but not with Galpha(s) subunits, competing with parathyroid hormone receptor for coupling to Galpha(q).
Role of scaffold protein afadin dilute domain-interacting protein (ADIP) in platelet-derived growth factor-induced cell movement by activating Rac protein through Vav2 protein.
Ogita et al., Kōbe, Japan. In J Biol Chem, 2012
The results indicate that ADIP plays an essential role in PDGF-induced cell movement by interacting with afadin and Vav2 and regulating the activation of Rac.
A FRET-Based Biosensor for Imaging SYK Activities in Living Cells.
Zhu et al., Atlanta, United States. In Cell Mol Bioeng, 2011
It contains an N-terminal ECFP, SH2 domain, a peptide derived from a SYK substrate VAV2, and a C-terminal YPet.
Vav family Rho guanine nucleotide exchange factors regulate CD36-mediated macrophage foam cell formation.
Silverstein et al., Cleveland, United States. In J Biol Chem, 2011
CD36 contributes to activation of Vav-1, -2, and -3 in aortae from hyperlipidemic mice
Negative regulation of EGFR-Vav2 signaling axis by Cbl ubiquitin ligase controls EGF receptor-mediated epithelial cell adherens junction dynamics and cell migration.
Band et al., Omaha, United States. In J Biol Chem, 2011
Cbl ubiquitin ligase plays a critical role in the maintenance of AJs and suppression of cell migration through down-regulation of EGFR-Vav2 signaling.
Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake by inducing Vav2-RhoA-mediated cytoskeletal rearrangements.
Meyer et al., Berlin, Germany. In Plos Biol, 2009
Type IV pili producing Neisseria gonorrhoeae triggers a phosphotyrosine-dependent Cav1-Vav2-RhoA signaling cascade that elicits cytoskeletal rearrangements and effectively impedes bacterial uptake into host cells.
Structure and function of vav.
Fischer et al., Paris, France. In Cell Signal, 1996
However, recently an homologue of vav, which is widely expressed (vav2) has been identified.
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