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Titolo:
Vav family proteins couple to diverse cell surface receptors
Autore:
Moores, SL; Selfors, LM; Fredericks, J; Breit, T; Fujikawa, K; Alt, FW; Brugge, JS; Swat, W;
Indirizzi:
Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 ed, Dept Cell Biol, Boston, MA 02115 USA Harvard Univ, Sch Med, Dept Genet, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 ch Med, Dept Genet, Boston, MA 02115 USA Harvard Univ, Sch Med, Ctr Blood Res, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 Med, Ctr Blood Res, Boston, MA 02115 USA Harvard Univ, Sch Med, Dept Pediat, Childrens Hosp, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 at, Childrens Hosp, Boston, MA 02115 USA Harvard Univ, Sch Med, Howard Hughes Med Inst, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 rd Hughes Med Inst, Boston, MA 02115 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 17, volume: 20, anno: 2000,
pagine: 6364 - 6373
SICI:
0270-7306(200009)20:17<6364:VFPCTD>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
AFFINITY PHOSPHOTYROSYL PEPTIDE; GTP EXCHANGE FACTOR; NF-KAPPA-B; TYROSINE PHOSPHORYLATION; PROTOONCOGENE PRODUCT; T-CELL; SIGNALING PATHWAY; RHO-FAMILY; KINASE SYK; SH2 DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Brugge, JS Harvard Univ, Sch Med, Dept Cell Biol, 240 Longwood Ave, Boston, MA 02115 USA Harvard Univ 240 Longwood Ave Boston MA USA 02115 MA 02115 USA
Citazione:
S.L. Moores et al., "Vav family proteins couple to diverse cell surface receptors", MOL CELL B, 20(17), 2000, pp. 6364-6373

Abstract

Vav proteins are guanine nucleotide exchange factors for Rho family GTPases which activate pathways leading to actin cytoskeletal rearrangements and transcriptional alterations. Vav proteins contain several protein binding domains which can link cell surface receptors to downstream signaling proteins. Vav1 is expressed exclusively in hematopoietic cells and tyrosine phosphorylated in response to activation of multiple cell surface receptors. However, it is not known whether the recently identified isoforms Vav2 and Vav3, which are broadly expressed, can couple,vith similar classes of receptors, nor is it known whether all Vav isoforms possess identical functional activities. We expressed Vav1, Vav2, and Vav3 at equivalent levels to directly compare the responses of the Vav proteins to receptor activation. Although each Vav isoform was tyrosine phosphorylated upon activation of representative receptor tyrosine kinases, integrin, and lymphocyte antigen receptors, we found unique aspects of Vav protein coupling in each receptor pathway. Each Vav protein coprecipitated with activated epidermal growth factor andplatelet-derived growth factor (PDGF) receptors, and multiple phosphorylated tyrosine residues on the PDGF receptor were able to mediate Vav2 tyrosine phosphorylation, Integrin-induced tyrosine phosphorylation of Vav proteins was net detected in nonhematopoietic cells unless the protein tyrosine kinase Syk was also expressed, suggesting that integrin activation of Vav proteins may be restricted to cell types that express particular tyrosine kinases. In addition, we found that Vav1, but not Vav2 or Vav3, can efficientlycooperate with T-cell receptor signaling to enhance NFAT dependent transcription, while Vav1 and Vav3, but not Vav2, can enhance NF kappa B dependenttranscription. Thus, although each Vav isoform can respond to similar cellsurface receptors, there are isoform-specific differences in their activation of downstream signaling pathways.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 09:14:24