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Gene Review

VAV1  -  vav 1 guanine nucleotide exchange factor

Homo sapiens

Synonyms: Proto-oncogene vav, VAV
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Disease relevance of VAV1

  • Ectopic expression of VAV1 reveals an unexpected role in pancreatic cancer tumorigenesis [1].
  • We show that melanoma cells express Vav1 and Vav2, which are activated by CXCL12 involving Jak activity [2].
  • Because Vav1 inducibly associates with further proteins including phospholipase C (PLC)gamma1 and Src homology 2 domain-containing leukocyte phosphoprotein of 76 kDa (SLP-76), we investigated their role for NF-kappaB activation in Jurkat leukemia T cell lines deficient for expression of these two proteins [3].
  • We also analysed the expression of Vav1 in 42 specimens of human neuroblastoma [4].
  • Overexpression was not observed in B-ALL or CMD, but 13% of B-NHL and 34.4% of B-CLL patients (P = 0.002) overexpressed VAV [5].

High impact information on VAV1


Chemical compound and disease context of VAV1

  • When another, AVP-antagonist, d(CH2)5-D-Tyr (Et) VAVP, which blocks vascular and renal tubular AVP-receptors, was administered chronically, the development of DOCA/salt hypertension was prevented at the expense of severe and persistent hypernatremia [10].

Biological context of VAV1


Anatomical context of VAV1


Associations of VAV1 with chemical compounds


Physical interactions of VAV1

  • Vav1 couples T cell receptor to serum response factor-dependent transcription via a MEK-dependent pathway [12].
  • Here we show that Vav1 also induces transcription factors that bind to the CD28RE/AP element contained in the interleukin-2 promoter [23].

Regulatory relationships of VAV1


Other interactions of VAV1

  • Adhesions in flow chambers and soluble binding assays using these transfectants indicated that initial ligand binding and adhesion strengthening mediated by alpha4beta1 were dependent on Vav1 and Rac activation by CXCL12 [11].
  • Although the role of Vav1 in T cells is well documented, the role of Vav3 is less clear [24].
  • Recognition and activation of Rho GTPases by Vav1 and Vav2 guanine nucleotide exchange factors [25].
  • Distinct functions of Vav1 in JNK1 activation in Jurkat T cells versus non-haematopoietic cells [14].
  • Binding of activation receptor 2B4 to its ligand CD48 was not sufficient for Vav1 phosphorylation [17].

Analytical, diagnostic and therapeutic context of VAV1


  1. Ectopic expression of VAV1 reveals an unexpected role in pancreatic cancer tumorigenesis. Fernandez-Zapico, M.E., Gonzalez-Paz, N.C., Weiss, E., Savoy, D.N., Molina, J.R., Fonseca, R., Smyrk, T.C., Chari, S.T., Urrutia, R., Billadeau, D.D. Cancer Cell (2005) [Pubmed]
  2. Activation of Vav/Rho GTPase signaling by CXCL12 controls membrane-type matrix metalloproteinase-dependent melanoma cell invasion. Bartolomé, R.A., Molina-Ortiz, I., Samaniego, R., Sánchez-Mateos, P., Bustelo, X.R., Teixidó, J. Cancer Res. (2006) [Pubmed]
  3. Src homology 2 domain-containing leukocyte phosphoprotein of 76 kDa and phospholipase C gamma 1 are required for NF-kappa B activation and lipid raft recruitment of protein kinase C theta induced by T cell costimulation. Dienz, O., Möller, A., Strecker, A., Stephan, N., Krammer, P.H., Dröge, W., Schmitz, M.L. J. Immunol. (2003) [Pubmed]
  4. The haematopoietic specific signal transducer Vav1 is expressed in a subset of human neuroblastomas. Hornstein, I., Pikarsky, E., Groysman, M., Amir, G., Peylan-Ramu, N., Katzav, S. J. Pathol. (2003) [Pubmed]
  5. Overexpression of the VAV proto-oncogene product is associated with B-cell chronic lymphocytic leukaemia displaying loss on 13q. Prieto-Sánchez, R.M., Hernández, J.A., García, J.L., Gutiérrez, N.C., San Miguel, J., Bustelo, X.R., Hernández, J.M. Br. J. Haematol. (2006) [Pubmed]
  6. VAV's got rhythm. Baylis, H.A. Cell (2005) [Pubmed]
  7. CD28 signaling via VAV/SLP-76 adaptors: regulation of cytokine transcription independent of TCR ligation. Raab, M., Pfister, S., Rudd, C.E. Immunity (2001) [Pubmed]
  8. Cbl-b is a negative regulator of receptor clustering and raft aggregation in T cells. Krawczyk, C., Bachmaier, K., Sasaki, T., Jones, R.G., Snapper, S.B., Bouchard, D., Kozieradzki, I., Ohashi, P.S., Alt, F.W., Penninger, J.M. Immunity (2000) [Pubmed]
  9. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Wu, J., Motto, D.G., Koretzky, G.A., Weiss, A. Immunity (1996) [Pubmed]
  10. The significance of vasopressin as a pressor agent. Hofbauer, K.G., Studer, W., Mah, S.C., Michel, J.B., Wood, J.M., Stalder, R. J. Cardiovasc. Pharmacol. (1984) [Pubmed]
  11. Vav1 and Rac control chemokine-promoted T lymphocyte adhesion mediated by the integrin alpha4beta1. García-Bernal, D., Wright, N., Sotillo-Mallo, E., Nombela-Arrieta, C., Stein, J.V., Bustelo, X.R., Teixidó, J. Mol. Biol. Cell (2005) [Pubmed]
  12. Vav1 couples T cell receptor to serum response factor-dependent transcription via a MEK-dependent pathway. Charvet, C., Auberger, P., Tartare-Deckert, S., Bernard, A., Deckert, M. J. Biol. Chem. (2002) [Pubmed]
  13. Tyrosine phosphorylation of adaptor protein 3BP2 induces T cell receptor-mediated activation of transcription factor. Qu, X., Kawauchi-Kamata, K., Miah, S.M., Hatani, T., Yamamura, H., Sada, K. Biochemistry (2005) [Pubmed]
  14. Distinct functions of Vav1 in JNK1 activation in Jurkat T cells versus non-haematopoietic cells. Kaminski, S., Del Pozo, M.A., Hipskind, R.A., Altman, A., Villalba, M. Scand. J. Immunol. (2004) [Pubmed]
  15. Defective Vav expression and impaired F-actin reorganization in a subset of patients with common variable immunodeficiency characterized by T-cell defects. Paccani, S.R., Boncristiano, M., Patrussi, L., Ulivieri, C., Wack, A., Valensin, S., Hirst, T.R., Amedei, A., Del Prete, G., Telford, J.L., D'Elios, M.M., Baldari, C.T. Blood (2005) [Pubmed]
  16. The adaptor protein 3BP2 associates with VAV guanine nucleotide exchange factors to regulate NFAT activation by the B-cell antigen receptor. Foucault, I., Le Bras, S., Charvet, C., Moon, C., Altman, A., Deckert, M. Blood (2005) [Pubmed]
  17. Vav1 phosphorylation is induced by beta2 integrin engagement on natural killer cells upstream of actin cytoskeleton and lipid raft reorganization. Riteau, B., Barber, D.F., Long, E.O. J. Exp. Med. (2003) [Pubmed]
  18. Vav2 activates Rac1, Cdc42, and RhoA downstream from growth factor receptors but not beta1 integrins. Liu, B.P., Burridge, K. Mol. Cell. Biol. (2000) [Pubmed]
  19. Vav1 and Ly-GDI two regulators of Rho GTPases, function cooperatively as signal transducers in T cell antigen receptor-induced pathways. Groysman, M., Hornstein, I., Alcover, A., Katzav, S. J. Biol. Chem. (2002) [Pubmed]
  20. Vav family proteins couple to diverse cell surface receptors. Moores, S.L., Selfors, L.M., Fredericks, J., Breit, T., Fujikawa, K., Alt, F.W., Brugge, J.S., Swat, W. Mol. Cell. Biol. (2000) [Pubmed]
  21. Tethered ligand-derived peptides of proteinase-activated receptor 3 (PAR3) activate PAR1 and PAR2 in Jurkat T cells. Hansen, K.K., Saifeddine, M., Hollenberg, M.D. Immunology (2004) [Pubmed]
  22. The Rac effector p67phox regulates phagocyte NADPH oxidase by stimulating Vav1 guanine nucleotide exchange activity. Ming, W., Li, S., Billadeau, D.D., Quilliam, L.A., Dinauer, M.C. Mol. Cell. Biol. (2007) [Pubmed]
  23. Tyrosine-phosphorylated Vav1 as a point of integration for T-cell receptor- and CD28-mediated activation of JNK, p38, and interleukin-2 transcription. Hehner, S.P., Hofmann, T.G., Dienz, O., Droge, W., Schmitz, M.L. J. Biol. Chem. (2000) [Pubmed]
  24. Membrane localization and function of Vav3 in T cells depend on its association with the adapter SLP-76. Charvet, C., Canonigo, A.J., Billadeau, D.D., Altman, A. J. Biol. Chem. (2005) [Pubmed]
  25. Recognition and activation of Rho GTPases by Vav1 and Vav2 guanine nucleotide exchange factors. Heo, J., Thapar, R., Campbell, S.L. Biochemistry (2005) [Pubmed]
  26. Protein kinase C theta cooperates with Vav1 to induce JNK activity in T-cells. Möller, A., Dienz, O., Hehner, S.P., Dröge, W., Schmitz, M.L. J. Biol. Chem. (2001) [Pubmed]
  27. The human VAV proto-oncogene maps to chromosome region 19p12----19p13.2. Martinerie, C., Cannizzaro, L.A., Croce, C.M., Huebner, K., Katzav, S., Barbacid, M. Hum. Genet. (1990) [Pubmed]
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