Regulation of Vav proteins by intramolecular events
- PMID: 11779690
- DOI: 10.2741/A766
Regulation of Vav proteins by intramolecular events
Abstract
The Vav family is a group of signal transduction molecules with oncogenic potential that play important roles in development and cell signaling. The function of Vav proteins co-evolved with tyrosine kinase pathways, probably to assure the optimal conversion of extracellular signals into intracellular responses coupled to the cytoskeleton and the transcriptome. To date, the best-known function of Vav proteins is their role as GDP/GTP exchange factors for Rho/Rac molecules. This activity is highly regulated during signal transduction by processes involving intramolecular interactions among several domains of Vav proteins. On one hand, the phosphorylation of Vav proteins on a specific tyrosine residue leads to a conformational change that allows the activation of the catalytic activity of Vav proteins. This mechanism of activation has been recently explained in structural terms and shown to involve the acidic and Dbl-homology domains of Vav. On the other hand, the activity of Vav proteins is affected by a second type of intramolecular interaction occurring between the plekstrin-homology and the catalytic regions of Vav that is regulated by phospholipids. In this review, we will give a brief overview of the recent advances in this field.
Similar articles
-
Vav proteins, adaptors and cell signaling.Oncogene. 2001 Oct 1;20(44):6372-81. doi: 10.1038/sj.onc.1204780. Oncogene. 2001. PMID: 11607839 Review.
-
Control of intramolecular interactions between the pleckstrin homology and Dbl homology domains of Vav and Sos1 regulates Rac binding.J Biol Chem. 2000 May 19;275(20):15074-81. doi: 10.1074/jbc.M907269199. J Biol Chem. 2000. PMID: 10748082
-
Rac-1 dependent stimulation of the JNK/SAPK signaling pathway by Vav.Oncogene. 1996 Aug 1;13(3):455-60. Oncogene. 1996. PMID: 8760286
-
Vav family proteins couple to diverse cell surface receptors.Mol Cell Biol. 2000 Sep;20(17):6364-73. doi: 10.1128/MCB.20.17.6364-6373.2000. Mol Cell Biol. 2000. PMID: 10938113 Free PMC article.
-
The VAV family of signal transduction molecules.Crit Rev Oncog. 1996;7(1-2):65-88. doi: 10.1615/critrevoncog.v7.i1-2.50. Crit Rev Oncog. 1996. PMID: 9109498 Review.
Cited by
-
High nuclear level of Vav1 is a positive prognostic factor in early invasive breast tumors: a role in modulating genes related to the efficiency of metastatic process.Oncotarget. 2014 Jun 30;5(12):4320-36. doi: 10.18632/oncotarget.2011. Oncotarget. 2014. PMID: 24962430 Free PMC article.
-
Expression of VAV1 in the tumour microenvironment of glioblastoma multiforme.J Neurooncol. 2012 Oct;110(1):69-77. doi: 10.1007/s11060-012-0936-y. Epub 2012 Aug 4. J Neurooncol. 2012. PMID: 22864683
-
Rho guanine nucleotide exchange factors: regulators of Rho GTPase activity in development and disease.Oncogene. 2014 Jul 31;33(31):4021-35. doi: 10.1038/onc.2013.362. Epub 2013 Sep 16. Oncogene. 2014. PMID: 24037532 Free PMC article. Review.
-
Age-related changes in lck-Vav signaling pathways in mouse CD4 T cells.Cell Immunol. 2009;259(1):100-4. doi: 10.1016/j.cellimm.2009.06.001. Epub 2009 Jun 6. Cell Immunol. 2009. PMID: 19577230 Free PMC article.
-
Vav mediates Ras stimulation by direct activation of the GDP/GTP exchange factor Ras GRP1.EMBO J. 2003 Jul 1;22(13):3326-36. doi: 10.1093/emboj/cdg316. EMBO J. 2003. PMID: 12839994 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Miscellaneous