Biology:VAV1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Proto-oncogene vav is a protein that in humans is encoded by the VAV1 gene.[1]

Function

The protein encoded by this proto-oncogene is a member of the Dbl family of guanine nucleotide exchange factors (GEF) for the Rho family of GTP binding proteins. The protein is important in hematopoiesis, playing a role in T-cell and B-cell development and activation. This particular GEF has been identified as the specific binding partner of Nef proteins from HIV-1. Coexpression and binding of these partners initiates profound morphological changes, cytoskeletal rearrangements and the JNK/SAPK signaling cascade, leading to increased levels of viral transcription and replication.[2]

Interactions

VAV1 has been shown to interact with:


References

  1. "Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav". Science 279 (5350): 558–60. February 1998. doi:10.1126/science.279.5350.558. PMID 9438848. Bibcode1998Sci...279..558H. 
  2. "Entrez Gene: VAV1 vav 1 oncogene". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7409. 
  3. "Vav, a GDP/GTP nucleotide exchange factor, interacts with GDIs, proteins that inhibit GDP/GTP dissociation". FEBS Lett. 467 (1): 75–80. February 2000. doi:10.1016/S0014-5793(00)01121-2. PMID 10664460. 
  4. "Association of Bcr-Abl with the proto-oncogene Vav is implicated in activation of the Rac-1 pathway". J. Biol. Chem. 277 (14): 12437–45. April 2002. doi:10.1074/jbc.M112397200. PMID 11790798. 
  5. 5.0 5.1 "Requirement of tyrosine-phosphorylated Vav for morphological differentiation of all-trans-retinoic acid-treated HL-60 cells". Cell Growth Differ. 12 (4): 193–200. April 2001. PMID 11331248. 
  6. "Proto-oncoprotein Vav interacts with c-Cbl in activated thymocytes and peripheral T cells". J. Immunol. 159 (1): 70–6. July 1997. PMID 9200440. 
  7. "Interaction of Vav with ENX-1, a putative transcriptional regulator of homeobox gene expression". Mol. Cell. Biol. 16 (6): 3066–73. June 1996. doi:10.1128/MCB.16.6.3066. PMID 8649418. 
  8. 8.0 8.1 "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways". Mol. Cell. Biol. 19 (5): 3798–807. May 1999. doi:10.1128/MCB.19.5.3798. PMID 10207103. 
  9. 9.0 9.1 9.2 "Association of a p95 Vav-containing signaling complex with the FcepsilonRI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex". J. Biol. Chem. 271 (43): 26962–70. October 1996. doi:10.1074/jbc.271.43.26962. PMID 8900182. 
  10. "Binding of Vav to Grb2 through dimerization of Src homology 3 domains". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12629–33. Dec 1994. doi:10.1073/pnas.91.26.12629. PMID 7809090. Bibcode1994PNAS...9112629Y. 
  11. 11.0 11.1 "Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6". FEBS Lett. 401 (2–3): 133–7. January 1997. doi:10.1016/s0014-5793(96)01456-1. PMID 9013873. 
  12. 12.0 12.1 "Role of the vav proto-oncogene product (Vav) in erythropoietin-mediated cell proliferation and phosphatidylinositol 3-kinase activity". J. Biol. Chem. 272 (22): 14334–40. May 1997. doi:10.1074/jbc.272.22.14334. PMID 9162069. 
  13. "Tyrosine phosphorylation of p95Vav in myeloid cells is regulated by GM-CSF, IL-3 and steel factor and is constitutively increased by p210BCR/ABL". EMBO J. 14 (2): 257–65. January 1995. doi:10.1002/j.1460-2075.1995.tb06999.x. PMID 7530656. 
  14. "p95vav associates with the nuclear protein Ku-70". Mol. Cell. Biol. 16 (1): 37–44. January 1996. doi:10.1128/mcb.16.1.37. PMID 8524317. 
  15. "Mapping the Zap-70 phosphorylation sites on LAT (linker for activation of T cells) required for recruitment and activation of signalling proteins in T cells". Biochem. J. 356 (Pt 2): 461–71. June 2001. doi:10.1042/0264-6021:3560461. PMID 11368773. 
  16. "Phosphorylation of the linker for activation of T-cells by Itk promotes recruitment of Vav". Biochemistry 41 (34): 10732–40. August 2002. doi:10.1021/bi025554o. PMID 12186560. 
  17. "Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCR zeta/CD3 induction of interleukin-2". Immunity 6 (2): 155–64. February 1997. doi:10.1016/s1074-7613(00)80422-7. PMID 9047237. 
  18. "Differential regulation of activation-induced tyrosine phosphorylation and recruitment of SLP-76 to Vav by distinct isoforms of the CD45 protein-tyrosine phosphatase". J. Biol. Chem. 271 (36): 22225–30. September 1996. doi:10.1074/jbc.271.36.22225. PMID 8703037. 
  19. 19.0 19.1 "Nuclear association of tyrosine-phosphorylated Vav to phospholipase C-gamma1 and phosphoinositide 3-kinase during granulocytic differentiation of HL-60 cells". FEBS Lett. 441 (3): 480–4. Dec 1998. doi:10.1016/s0014-5793(98)01593-2. PMID 9891995. 
  20. "Vav synergizes with protein kinase C theta to mediate IL-4 gene expression in response to CD28 costimulation in T cells". J. Immunol. 164 (7): 3829–36. April 2000. doi:10.4049/jimmunol.164.7.3829. PMID 10725744. 
  21. "Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions". Mol. Cell 3 (6): 729–39. June 1999. doi:10.1016/S1097-2765(01)80005-8. PMID 10394361. 
  22. "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells". Eur. J. Biochem. 269 (13): 3279–88. July 2002. doi:10.1046/j.1432-1033.2002.03008.x. PMID 12084069. 
  23. "Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product". Immunity 5 (6): 591–604. Dec 1996. doi:10.1016/s1074-7613(00)80273-3. PMID 8986718. 

Further reading