Biology:VAV1
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Short description: Protein-coding gene in the species Homo sapiens
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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:
- ARHGDIB,[3]
- Abl gene,[4]
- Cbl gene[5][6]
- EZH2,[7]
- Grb2,[8][9][10][11]
- JAK2,[12][13]
- Ku70,[14]
- LAT,[15][16]
- LCP2,[17][18]
- MAPK1,[9][11]
- PIK3R1,[12][19]
- PLCG1,[19]
- PRKCQ,[20]
- S100B,[21]
- SHB,[22]
- SIAH2,[8] and
- Syk.[5][9][23]
References
- ↑ "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. Bibcode: 1998Sci...279..558H.
- ↑ "Entrez Gene: VAV1 vav 1 oncogene". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7409.
- ↑ "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.
- ↑ "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.
- ↑ 5.0 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.
- ↑ "Proto-oncoprotein Vav interacts with c-Cbl in activated thymocytes and peripheral T cells". J. Immunol. 159 (1): 70–6. July 1997. PMID 9200440.
- ↑ "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.
- ↑ 8.0 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.
- ↑ 9.0 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.
- ↑ "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. Bibcode: 1994PNAS...9112629Y.
- ↑ 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.
- ↑ 12.0 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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ 19.0 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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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
- "Structure and function of vav". Cell. Signal. 8 (8): 545–53. 1997. doi:10.1016/S0898-6568(96)00118-0. PMID 9115846.
- "Regulatory and Signaling Properties of the Vav Family". Mol. Cell. Biol. 20 (5): 1461–77. 2000. doi:10.1128/MCB.20.5.1461-1477.2000. PMID 10669724.
- "Structure–function relationships in HIV-1 Nef". EMBO Rep. 2 (7): 580–5. 2001. doi:10.1093/embo-reports/kve141. PMID 11463741.
- "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication". J. Biosci. 28 (3): 323–35. 2004. doi:10.1007/BF02970151. PMID 12734410.
- "HIV accessory proteins and surviving the host cell". Current HIV/AIDS Reports 1 (1): 47–53. 2005. doi:10.1007/s11904-004-0007-x. PMID 16091223.
- "Modelling thymic HIV-1 Nef effects". Curr. HIV Res. 4 (1): 57–64. 2006. doi:10.2174/157016206775197583. PMID 16454711.
- "Flesh and blood: the story of Vav1, a gene that signals in hematopoietic cells but can be transforming in human malignancies". Cancer Lett. 255 (2): 241–54. 2007. doi:10.1016/j.canlet.2007.04.015. PMID 17590270.
- "Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells". Science 256 (5060): 1196–9. 1992. doi:10.1126/science.256.5060.1196. PMID 1375396. Bibcode: 1992Sci...256.1196B.
- "The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization". Oncogene 7 (4): 611–8. 1992. PMID 1565462.
- "Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential". Mol. Cell. Biol. 11 (4): 1912–20. 1991. doi:10.1128/MCB.11.4.1912. PMID 2005887.
- "Mechanism of activation of the vav protooncogene". Cell Growth Differ. 2 (2): 95–105. 1991. PMID 2069873.
- "vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells". EMBO J. 8 (8): 2283–90. 1989. doi:10.1002/j.1460-2075.1989.tb08354.x. PMID 2477241.
- "The proline-rich region of Vav binds to Grb2 and Grb3-3". Oncogene 11 (8): 1665–9. 1995. PMID 7478592.
- "Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors". J. Biol. Chem. 269 (51): 32514–21. 1995. doi:10.1016/S0021-9258(18)31664-8. PMID 7528218.
- "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. 1995. doi:10.1002/j.1460-2075.1995.tb06999.x. PMID 7530656.
- "Insulin-dependent tyrosine phosphorylation of the vav protooncogene product in cells of hematopoietic origin". J. Biol. Chem. 270 (13): 7712–6. 1995. doi:10.1074/jbc.270.13.7712. PMID 7535775.
- "Interleukin 3 and erythropoietin induce association of Vav with Tec kinase through Tec homology domain". Oncogene 11 (4): 619–25. 1995. PMID 7651724.
- "Vav is necessary for prolactin-stimulated proliferation and is translocated into the nucleus of a T-cell line". J. Biol. Chem. 270 (22): 13246–53. 1995. doi:10.1074/jbc.270.22.13246. PMID 7768923.
- "The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav". J. Biol. Chem. 269 (51): 32579–85. 1995. doi:10.1016/S0021-9258(18)31673-9. PMID 7798261.
- "Binding of Vav to Grb2 through dimerization of Src homology 3 domains". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12629–33. 1995. doi:10.1073/pnas.91.26.12629. PMID 7809090. Bibcode: 1994PNAS...9112629Y.
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