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Titolo:
Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility
Autore:
Sanjay, A; Houghton, A; Neff, L; DiDomenico, E; Bardelay, C; Antoine, E; Levy, J; Gailit, J; Bowtell, D; Horne, WC; Baron, R;
Indirizzi:
Yale Univ, Sch Med, Dept Cell Biol & Orthoped, New Haven, CT 06510 USA Yale Univ New Haven CT USA 06510 Biol & Orthoped, New Haven, CT 06510 USA Hoechst Marion Roussel, Bone Dis Grp, F-93235 Romainville, France Hoechst Marion Roussel Romainville France F-93235 35 Romainville, France SUNY Stony Brook, Jules Wellton Rheingold Texas Res Fdn, Stony Brook, NY 11790 USA SUNY Stony Brook Stony Brook NY USA 11790 Fdn, Stony Brook, NY 11790 USA Peter MacCallum Canc Inst, E Melbourne, Vic 3002, Australia Peter MacCallum Canc Inst E Melbourne Vic Australia 3002 3002, Australia
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 1, volume: 152, anno: 2001,
pagine: 181 - 195
SICI:
0021-9525(20010108)152:1<181:CAWPAS>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR RECEPTOR; VIRUS-TRANSFORMED FIBROBLASTS; PROTOONCOGENE C-CBL; SYK TYROSINE KINASE; EXPRESS HIGH-LEVELS; NEGATIVE REGULATOR; FAMILY KINASES; ADAPTER PROTEIN; DEFICIENT MICE; RING FINGER;
Keywords:
Cbl; Src; Pyk2; osteoclast; vitronectin receptor (alpha(v)beta(3));
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Baron, R Yale Univ, Sch Med, Dept Cell Biol & Orthoped, POB 208044, New Haven, CT 06510 USA Yale Univ POB 208044 New Haven CT USA 06510 w Haven, CT 06510 USA
Citazione:
A. Sanjay et al., "Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility", J CELL BIOL, 152(1), 2001, pp. 181-195

Abstract

The signaling events downstream of integrins that regulate cell attachmentand motility are only partially understood. Using osteoclasts and transfected 293 cells, we find that a molecular complex comprising Src, Pyk2, and Cbl functions to regulate cell adhesion and motility. The activation of integrin alpha (v)beta (3) induces the [Ca2+](i)-dependent phosphorylation of Pyk2 Y402, its association with Src SH2, Src activation, and the Src SH3-dependent recruitment and phosphorylation of c-Cbl. Furthermore, the PTB domain of Cbl is shown to bind to phosphorylated Tyr-416 in the activation loop ofSrc, the autophosphorylation site of Src, inhibiting Src kinase activity and integrin-mediated adhesion. Finally, we show that deletion of c Src or c-Cbl leads to a decrease in osteoclast migration. Thus, binding of a,Ps integrin induces the formation of a Pyk2/Src/Cbl complex in which Cbl is a key regulator of Src kinase activity and of cell adhesion and migration. These findings may explain the osteopetrotic phenotype in the Src(-/-) mice.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 22:44:28