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Titolo:
Activation of Syk protein tyrosine kinase through interaction with integrin beta cytoplasmic domains
Autore:
Woodside, DG; Obergfell, A; Leng, L; Wilsbacher, JL; Miranti, CK; Brugge, JS; Shattil, SJ; Ginsberg, MH;
Indirizzi:
Scripps Res Inst, Dept Vasc Biol, La Jolla, CA 92037 USA Scripps Res InstLa Jolla CA USA 92037 Vasc Biol, La Jolla, CA 92037 USA Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA Scripps Res InstLa Jolla CA USA 92037 Cell Biol, La Jolla, CA 92037 USA Scripps Res Inst, Dept Mol & Expt Med, La Jolla, CA 92037 USA Scripps Res Inst La Jolla CA USA 92037 & Expt Med, La Jolla, CA 92037 USA 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
Titolo Testata:
CURRENT BIOLOGY
fascicolo: 22, volume: 11, anno: 2001,
pagine: 1799 - 1804
SICI:
0960-9822(20011113)11:22<1799:AOSPTK>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
HIGH-AFFINITY RECEPTOR; B-CELL DEVELOPMENT; ALPHA(IIB)BETA(3); PHOSPHORYLATION; ENGAGEMENT; PP72(SYK); P72(SYK); ADHESION; FAMILY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Ginsberg, MH Scripps Res Inst, Dept Vasc Biol, La Jolla, CA 92037 USA Scripps Res Inst La Jolla CA USA 92037 a Jolla, CA 92037 USA
Citazione:
D.G. Woodside et al., "Activation of Syk protein tyrosine kinase through interaction with integrin beta cytoplasmic domains", CURR BIOL, 11(22), 2001, pp. 1799-1804

Abstract

Syk protein tyrosine kinase is essential for immune system development andfunction [1] and for the maintenance of vascular integrity [2, 3]. In leukocytes, Syk is activated by binding to diphosphorylated immune receptor tyrosine-based activation motifs (pITAMs) [1]. Syk can also be activated by integrin adhesion receptors [4, 5], but the mechanism of its activation is unknown. Here we report a novel mechanism for Syk's recruitment and activation, which requires that Syk bind to the integrin beta3 cytoplasmic tail. We found that both Syk and the related kinase ZAP-70 bound the beta3 cytoplasmic tail through their tandem SH2 domains. However, unlike Syk binding to pITAMs, this interaction was independent of tyrosine phosphorylation and of the phosphotyrosine binding function of Syk's tandem SH2 domains. Deletion of the four C-terminal residues of the beta3 cytoplasmic tail [beta3(759X)] decreased Syk binding and disrupted its physical association with integrin alpha IIb beta3. Furthermore, cells expressing alpha IIbp3(759X) failed to exhibit Syk activation or lamellipodia formation upon cell adhesion to the alpha IIb beta3 ligand, fibrinogen. In contrast, FAK phosphorylation and focal adhesion formation were unimpaired by this mutation. Thus, the direct binding of Syk kinase to the integrin beta3 cytoplasmic tail is a novel and functionally significant mechanism for the regulation of this important non-receptor tyrosine kinase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/20 alle ore 07:48:28