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VAV3  -  vav 3 guanine nucleotide exchange factor

Homo sapiens

Synonyms: Guanine nucleotide exchange factor VAV3, VAV-3
 
 
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Disease relevance of VAV3

 

High impact information on VAV3

 

Chemical compound and disease context of VAV3

  • We observed a marked increase in the expression of Vav3, a Rho GTPase guanine nucleotide exchange factor (GEF), during the progression of human prostate cancer LNCaP cells to the androgen-independent derivative, LNCaP-R1 [4].
 

Biological context of VAV3

 

Anatomical context of VAV3

  • However, unlike, VAV, the VAV3 and VAV3.1 transcripts are also found at varying levels in a wide variety of other tissues and cell lines [5].
  • Vav3 induced marked membrane ruffles and microspikes in NIH 3T3 cells, while the N-terminal truncation mutants of Vav3 significantly enhanced membrane ruffle formation but had a reduced ability to induce microspikes [9].
  • We investigated the subcellular localization of Vav3 during T cell activation [8].
  • Strikingly, Vav3 was transiently up-regulated in HeLa cells during mitosis, whereas enforced expression of Vav3 perturbed cytokinesis and led to the appearance of multinucleated cells [3].
  • In mammals, there are three family members; Vav1 is specifically expressed in the hematopoietic system, whereas Vav2 and Vav3 are more ubiquitously expressed [10].
 

Associations of VAV3 with chemical compounds

  • Major transcript variants of VAV3, a new member of the VAV family of guanine nucleotide exchange factors [5].
  • These integrin-transmitted signals include activation of the associated proteins, c-src, syk, Vav3, and Rho GTPases [11].
  • In contrast, overexpression of Vav3 promoted androgen-independent growth of LNCaP cells induced by epidermal growth factor [1].
 

Regulatory relationships of VAV3

 

Other interactions of VAV3

  • Altogether, our data show that TCR-induced association of Vav3 with SLP-76 is required for its membrane/IS localization and function [8].
  • Focus formation assays demonstrated that APS could increase the transforming activity of proto-Vav3 [12].
 

Analytical, diagnostic and therapeutic context of VAV3

References

  1. Vav3 oncogene is overexpressed and regulates cell growth and androgen receptor activity in human prostate cancer. Dong, Z., Liu, Y., Lu, S., Wang, A., Lee, K., Wang, L.H., Revelo, M., Lu, S. Mol. Endocrinol. (2006) [Pubmed]
  2. Differential regulation of TCR-mediated gene transcription by Vav family members. Zakaria, S., Gomez, T.S., Savoy, D.N., McAdam, S., Turner, M., Abraham, R.T., Billadeau, D.D. J. Exp. Med. (2004) [Pubmed]
  3. Vav3 is regulated during the cell cycle and effects cell division. Fujikawa, K., Inoue, Y., Sakai, M., Koyama, Y., Nishi, S., Funada, R., Alt, F.W., Swat, W. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  4. Vav3, a Rho GTPase Guanine Nucleotide Exchange Factor, Increases during Progression to Androgen Independence in Prostate Cancer Cells and Potentiates Androgen Receptor Transcriptional Activity. Lyons, L.S., Burnstein, K.L. Mol. Endocrinol. (2006) [Pubmed]
  5. Major transcript variants of VAV3, a new member of the VAV family of guanine nucleotide exchange factors. Trenkle, T., McClelland, M., Adlkofer, K., Welsh, J. Gene (2000) [Pubmed]
  6. Bovine mammary gene expression profiling using a cDNA microarray enhanced for mammary-specific transcripts. Suchyta, S.P., Sipkovsky, S., Halgren, R.G., Kruska, R., Elftman, M., Weber-Nielsen, M., Vandehaar, M.J., Xiao, L., Tempelman, R.J., Coussens, P.M. Physiol. Genomics (2003) [Pubmed]
  7. Vav1 and vav3 have critical but redundant roles in mediating platelet activation by collagen. Pearce, A.C., Senis, Y.A., Billadeau, D.D., Turner, M., Watson, S.P., Vigorito, E. J. Biol. Chem. (2004) [Pubmed]
  8. 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]
  9. Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation. Zeng, L., Sachdev, P., Yan, L., Chan, J.L., Trenkle, T., McClelland, M., Welsh, J., Wang, L.H. Mol. Cell. Biol. (2000) [Pubmed]
  10. Vav proteins, masters of the world of cytoskeleton organization. Hornstein, I., Alcover, A., Katzav, S. Cell. Signal. (2004) [Pubmed]
  11. Osteoclasts: what do they do and how do they do it? Teitelbaum, S.L. Am. J. Pathol. (2007) [Pubmed]
  12. Adaptor protein APS binds the NH2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity. Yabana, N., Shibuya, M. Oncogene (2002) [Pubmed]
 
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