The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Vav2  -  vav 2 oncogene

Mus musculus

Synonyms: 2810040F13Rik, AI847175, Guanine nucleotide exchange factor VAV2, VAV-2
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Vav2

  • We report that this is the case for Vav2, because the disruption of its locus in mice causes tachycardia, hypertension, and defects in the heart, arterial walls, and kidneys [1].

High impact information on Vav2


Biological context of Vav2

  • Consistent with their distinct substrate targets, it was found that constitutively activated versions of Vav and Vav2 caused distinct transformed phenotypes when expressed in NIH 3T3 cells [4].
  • Transfection of NIH3T3 cells with expression vectors containing vav2 deletions demonstrate that elimination of 183 amino terminal residues of Vav2 is sufficient to activate its oncogenic potential [5].
  • Vav2-induced transformation is characterized by the appearance of foci composed of cells in which cytokinesis and karyokinesis are uncoupled [5].
  • Signal transduction through Vav-2 participates in humoral immune responses and B cell maturation [3].
  • In contrast, the constitutive expression of the Vav-2 oncoprotein in rodent fibroblasts leads to major alterations in cell morphology and to highly enlarged cells in which karyokinesis and cytokinesis frequently are uncoupled [6].

Anatomical context of Vav2

  • It is also possible that two other Vav family molecules, Vav2 and Vav3, are involved in NK cell activation [7].
  • To investigate whether Vav isoforms have redundant or unique functions in regulating adhesion and migration, we investigated the properties of Vav1-deficient and Vav2-deficient macrophages [8].
  • Both Vav1-deficient and Vav2-deficient cells have a smaller adhesive area; yet, only Vav1-deficient cells have a reduced migration speed, which coincides with a lower level of microtubules [8].
  • Finally, Vav2-transformed NIH 3T3 cells showed up-regulated levels of Rac-GTP [4].
  • Vav-2-deficient mice are also defective in their ability to switch immunoglobulin class, form germinal centers and generate secondary immune responses to TD antigens [3].

Associations of Vav2 with chemical compounds

  • Vav1-mutant mice generate defective humoral immunoglobulin G (IgG) responses following administration of low doses of LPS but respond normally to higher doses, while mice lacking both Vav1 and Vav2 manifest defective responses even after a high dose of LPS [9].
  • In vivo, wild-type Vav-2 is activated oncogenically by tyrosine kinases, an effect enhanced further by co-expression of RhoA [6].

Other interactions of Vav2


  1. Loss of Vav2 proto-oncogene causes tachycardia and cardiovascular disease in mice. Sauzeau, V., Jerkic, M., López-Novoa, J.M., Bustelo, X.R. Mol. Biol. Cell (2007) [Pubmed]
  2. Compensation between Vav-1 and Vav-2 in B cell development and antigen receptor signaling. Tedford, K., Nitschke, L., Girkontaite, I., Charlesworth, A., Chan, G., Sakk, V., Barbacid, M., Fischer, K.D. Nat. Immunol. (2001) [Pubmed]
  3. Signal transduction through Vav-2 participates in humoral immune responses and B cell maturation. Doody, G.M., Bell, S.E., Vigorito, E., Clayton, E., McAdam, S., Tooze, R., Fernandez, C., Lee, I.J., Turner, M. Nat. Immunol. (2001) [Pubmed]
  4. Vav2 is an activator of Cdc42, Rac1, and RhoA. Abe, K., Rossman, K.L., Liu, B., Ritola, K.D., Chiang, D., Campbell, S.L., Burridge, K., Der, C.J. J. Biol. Chem. (2000) [Pubmed]
  5. Isolation and characterization of murine vav2, a member of the vav family of proto-oncogenes. Schuebel, K.E., Bustelo, X.R., Nielsen, D.A., Song, B.J., Barbacid, M., Goldman, D., Lee, I.J. Oncogene (1996) [Pubmed]
  6. Phosphorylation-dependent and constitutive activation of Rho proteins by wild-type and oncogenic Vav-2. Schuebel, K.E., Movilla, N., Rosa, J.L., Bustelo, X.R. EMBO J. (1998) [Pubmed]
  7. Differential requirements for Vav proteins in DAP10- and ITAM-mediated NK cell cytotoxicity. Cella, M., Fujikawa, K., Tassi, I., Kim, S., Latinis, K., Nishi, S., Yokoyama, W., Colonna, M., Swat, W. J. Exp. Med. (2004) [Pubmed]
  8. Vav1 and Vav2 play different roles in macrophage migration and cytoskeletal organization. Wells, C.M., Bhavsar, P.J., Evans, I.R., Vigorito, E., Turner, M., Tybulewicz, V., Ridley, A.J. Exp. Cell Res. (2005) [Pubmed]
  9. Vav proteins are required for B-lymphocyte responses to LPS. Hebeis, B., Vigorito, E., Kovesdi, D., Turner, M. Blood (2005) [Pubmed]
  10. Tyrosine phosphorylation mediates both activation and downmodulation of the biological activity of Vav. López-Lago, M., Lee, H., Cruz, C., Movilla, N., Bustelo, X.R. Mol. Cell. Biol. (2000) [Pubmed]
WikiGenes - Universities