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Titolo:
The Shc adaptor protein forms interdependent phosphotyrosine-mediated protein complexes in mast cells stimulated with interleukin 3
Autore:
Velazquez, L; Gish, GD; van der Geer, P; Taylor, L; Shulman, J; Pawson, T;
Indirizzi:
Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Programme Mol Biol & Canc, Toronto, ON M5G 1X5, Canada Mt Sinai Hosp Toronto ON Canada M5G 1X5 Canc, Toronto, ON M5G 1X5, Canada Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 iochem, La Jolla, CA 92093 USA PE SCIEX, Concord, ON, Canada PE SCIEX Concord ON CanadaPE SCIEX, Concord, ON, Canada Univ Toronto, Dept Mol & Med Genet, Toronto, ON, Canada Univ Toronto Toronto ON Canada Dept Mol & Med Genet, Toronto, ON, Canada
Titolo Testata:
BLOOD
fascicolo: 1, volume: 96, anno: 2000,
pagine: 132 - 138
SICI:
0006-4971(20000701)96:1<132:TSAPFI>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
INOSITOL PHOSPHATASE SHIP; COMMON BETA-SUBUNIT; TYROSINE-PHOSPHORYLATED PROTEIN; SIGNAL-TRANSDUCTION; FACTOR-RECEPTOR; BINDING DOMAIN; PTB DOMAIN; HEMATOPOIETIC-CELLS; CYTOPLASMIC DOMAINS; MULTIPLE CYTOKINES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Pawson, T Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Programme Mol Biol & Canc, 600 Univ Ave, Toronto, ON M5G 1X5, Canada Mt Sinai Hosp 600 Univ Ave Toronto ON Canada M5G 1X5 1X5, Canada
Citazione:
L. Velazquez et al., "The Shc adaptor protein forms interdependent phosphotyrosine-mediated protein complexes in mast cells stimulated with interleukin 3", BLOOD, 96(1), 2000, pp. 132-138

Abstract

The Shc adaptor protein possesses 2 distinct phosphotyrosine (pTyr) recognition modules-the pTyr binding (PTB) domain and the Src homology 2 (SH2) domain-and multiple potential sites for tyrosine (Tyr) phosphorylation (Tyr residues 239, 240, and 317). On stimulation of hematopoietic cells with interleukin 3 (IL-3), Shc becomes phosphorylated and may therefore contribute to IL-3 signaling. We investigated the interactions mediated by the Shc modular domains and pTyr sites in IL-3-dependent IC2 premast cells. The Shc PTBdomain, rather than the SH2 domain, associated both in vitro end in vivo with the Tyr-phosphorylated beta subunit of the IL-3 receptor and with the SH2-containing 5' inositol phosphatase (SHIP), and it recognized specific NXXpY phosphopeptides from these binding partners. In IL-3-stimulated mast cells, Shc phosphorylation occurred primarily on Tyr239 and 317 and was dependent on a functional PTB domain. Phosphorylated Tyr317, and to a lesser extent, Tyr239, bound the Grb2 adaptor and SHIP. Furthermore, a pTyr317 Shc phosphopeptide selectively recognized Grb2, Sos1, SHIP, and the p85 subunit of phosphatidylinositol 3' kinase from mast cells, as characterized by mass spectrometry. These results indicate that Shc undergoes an interdependent series of pTyr-mediated interactions in IL-3-stimulated mast cells, resulting in the recruitment of proteins that regulate the Ras pathway and phospholipid metabolism. (Blood. 2000;96:132-138) (C) 2000 by The American Society of Hematology.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:30:12