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Titolo:
Tyrosine-phosphorylated SOCS-3 inhibits STAT activation but binds to p120 RasGAP and activates Ras
Autore:
Cacalano, NA; Sanden, D; Johnston, JA;
Indirizzi:
DNAX Res Inst Mol & Cellular Biol Inc, Res Inst, Palo Alto, CA 94304 USA DNAX Res Inst Mol & Cellular Biol Inc Palo Alto CA USA 94304 CA 94304 USA
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 5, volume: 3, anno: 2001,
pagine: 460 - 465
SICI:
1465-7392(200105)3:5<460:TSISAB>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR BETA-CHAIN; INDUCED PROLIFERATION; SIGNAL-TRANSDUCTION; SH2 DOMAIN; PROTEIN; INTERLEUKIN-2; MEDIATE; KINASE; JAKS; JAB;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Cacalano, NA Queens Univ Belfast, Dept Immunol, Whitla Med Bldg,97 LisburnRd, Belfast BT9 7BL, Antrim, North Ireland Queens Univ Belfast Whitla Med Bldg,97 Lisburn Rd Belfast Antrim North Ireland BT9 7BL
Citazione:
N.A. Cacalano et al., "Tyrosine-phosphorylated SOCS-3 inhibits STAT activation but binds to p120 RasGAP and activates Ras", NAT CELL BI, 3(5), 2001, pp. 460-465

Abstract

Suppressors of cytokine signalling (SOCS, also known as CIS and SSI) are encoded by immediate early genes that act in a feedback loop to inhibit cytokine responses and activation of 'signal transducer and activator of transcription' (STAT). Here we show that SOCS-3 is strongly tyrosine-phosphorylated in response to many growth factors, including interleukin-2 (IL-2), erythropoietin (EPO), epidermal growth factor (EGF) and platelet-derived growthfactor (PDGF). The principal phosphorylation sites on SOCS-3 are residues 204 and 221 at the carboxy terminus, and upon phosphorylation tyrosine 221 interacts with the Ras inhibitor p120 RasGAP. After IL-2 stimulation, phosphorylated SOCS-3 strongly inhibits STAT5 activation but, by binding to RasGAP, maintains activation of extracellular-signal-regulated kinase (ERK). A tyrosine mutant of SOCS-3 still blocks STAT phosphorylation, but also strongly inhibits IL-2-dependent activation of ERK and cell proliferation. Moreover, it also inhibits EPO- and PDGF-induced proliferation and ERK activation. Therefore, although SOCS proteins inhibit growth-factor responses, tyrosine phosphorylation of SOCS-3 can ensure cell survival and proliferation through the Ras pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 05:32:59