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Titolo:
The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1
Autore:
Chang, BY; Chiang, ML; Cartwright, CA;
Indirizzi:
Stanford Univ, Sch Med, Dept Med, Stanford, CA 94305 USA Stanford Univ Stanford CA USA 94305 Med, Dept Med, Stanford, CA 94305 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 23, volume: 276, anno: 2001,
pagine: 20346 - 20356
SICI:
0021-9258(20010608)276:23<20346:TIOSAR>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
BETA-GAMMA-SUBUNITS; ADRENERGIC-RECEPTOR KINASE; MIDDLE TUMOR-ANTIGEN; NIH 3T3 CELLS; WD-REPEAT; SIGNAL-TRANSDUCTION; SH2 DOMAIN; MONOCLONAL-ANTIBODIES; ANCHORING PROTEINS; SCAFFOLD PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Cartwright, CA Stanford Univ, Sch Med, Dept Med, CCSR Bldg,Rm 3115C,269 Campus Dr, Stanford, CA 94305 USA Stanford Univ CCSR Bldg,Rm 3115C,269 CampusDr Stanford CA USA 94305
Citazione:
B.Y. Chang et al., "The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1", J BIOL CHEM, 276(23), 2001, pp. 20346-20356

Abstract

RACK1 is an intracellular receptor for the serine/threonine protein kinaseC. Previously, we demonstrated that RACK1 also interacts with the Src protein-tyrosine kinase. RACK1, via its association with these protein kinases,may play a key role in signal transduction. To further characterize the Src-RACK1 interaction and to analyze mechanisms by which cross-talk occurs between the two RACK1-linked signaling kinases, we identified sites on Src and RACK1 that mediate their binding, and factors that regulate their interaction. We found that the interaction of Src and RACK1 is mediated, in part, by the SH2 domain of Src and by phosphotyrosines in the sixth WD repeat of RACK1, and is enhanced by serum or platelet-derived growth factor stimulation, protein kinase C activation, and tyrosine phosphorylation of RACK1. To the best of our knowledge, this is the first report of tyrosine phosphorylation of a member of the WD repeat family of proteins. We think that tyrosine phosphorylation of these proteins is an important mechanism of signal transduction in cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 06:58:49