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Titolo:
Hepatocyte Growth Factor/Scatter Factor-induces phosphorylation of cortactin in A431 cells in a Src kinase-independent manner
Autore:
Crostella, L; Lidder, S; Williams, R; Skouteris, GG;
Indirizzi:
Royal Free & Univ Coll London, Sch Med, Dept Med, Inst Hepatol,Lab Cell Biol, London WC1E 6HX, England Royal Free & Univ Coll London London EnglandWC1E 6HX WC1E 6HX, England
Titolo Testata:
ONCOGENE
fascicolo: 28, volume: 20, anno: 2001,
pagine: 3735 - 3745
SICI:
0950-9232(20010621)20:28<3735:HGFFPO>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR TYROSINE KINASE; GRB2 BINDING-SITE; SCATTER FACTOR; MET RECEPTOR; C-MET; EPITHELIAL-CELLS; CARCINOMA-CELLS; V-SRC; MOTILITY; PROTEIN;
Keywords:
tyrosine phosphorylation; MET; F-actin binding proteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Skouteris, GG Royal Free & UCL Med Sch, Dept Med, Ctr Hepatol, Lab Cellular & Mol Biol, Upper 3rd Floor,Rowland Hill St,Royal Free Campus, London NW32PF, England Royal Free & UCL Med Sch Upper 3rd Floor,Rowland Hill St,Royal Free Campus London England NW3 2PF
Citazione:
L. Crostella et al., "Hepatocyte Growth Factor/Scatter Factor-induces phosphorylation of cortactin in A431 cells in a Src kinase-independent manner", ONCOGENE, 20(28), 2001, pp. 3735-3745

Abstract

The Hepatocyte Growth Factor receptor transduces proliferating and scattering signals in epithelial and endothelial cells. We have explored potentialinteractions of the HGF/SF receptor beta-subunit (p145(beta MET)) with F-actin binding partners aiming to identify novel downstream effecters implicated in HGF/SF pluripotent signalling. Cortactin, a p80/85 F-actin binding protein, was found phosphorylated on tyrosine in response to HGF-SF in A431 human epidermoid carcinoma cells, expressing the HGF/SF receptor (c-MET). The HGF/SF receptor was enriched in the detergent-insoluble fraction and wasfound to co-precipitate with cortactin and to associate in vitro with cortactin, The Grb2 small adapter protein known to associate via its Src homology 2 domain (SH2) with the MET C-terminus, was also associated with cortactin, Transient transfection of A431 cells with dominant-negative Grb2 constructs has revealed that the Grb2-C-SH3 domain possesses central role in cortactin phosphorylation in response to HGF/SF, Finally, tyrosine phosphorylation of cortactin was found uncoupled of endogenous c-Src kinase activity, thus further supporting the hypothesis that cortactin is a direct target of the MET kinase, We propose that cortactin may constitute a docking site forMET-derived signals within the cytoskeleton.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 21:29:31