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Titolo:
Association of p130(CAS) with phosphatidylinositol-3-OH kinase mediates adenovirus cell entry
Autore:
Li, EG; Stupack, DG; Brown, SL; Klemke, R; Schlaepfer, DD; Nemerow, GR;
Indirizzi:
Scripps Clin & Res Inst, Dept Immunol, La Jolla, CA 92037 USA Scripps Clin& Res Inst La Jolla CA USA 92037 nol, La Jolla, CA 92037 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 19, volume: 275, anno: 2000,
pagine: 14729 - 14735
SICI:
0021-9258(20000512)275:19<14729:AOPWPK>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
FOCAL ADHESION KINASE; PROTEIN-TYROSINE-PHOSPHATASE; DIRECT BINDING; GROWTH-FACTOR; PHOSPHOINOSITIDE-3-OH KINASE; SUBSTRATE P130(CAS); ALPHA(V) INTEGRINS; SH3 DOMAINS; SRC KINASE; IN-VIVO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Nemerow, GR Scripps Clin & Res Inst, Dept Immunol, 10550 N Torrey Pines Rd, La Jolla, CA 92037 USA Scripps Clin & Res Inst 10550 N Torrey Pines Rd LaJolla CA USA 92037
Citazione:
E.G. Li et al., "Association of p130(CAS) with phosphatidylinositol-3-OH kinase mediates adenovirus cell entry", J BIOL CHEM, 275(19), 2000, pp. 14729-14735

Abstract

The Crk-associated substrate, p130(CAS), has been implicated in the regulation of the actin cytoskeleton following ligation of cell integrins with the extracellular matrix. Integrin-mediated cell adhesion involves p130(CAS) association with focal adhesion kinase (p125(FAK)). Internalization/cell entry of type 2 and type 5 adenoviruses (Ad) is also mediated by alpha(v) integrins. However, expression of dominant negative forms of p125FAK does not alter virus entry, and Ad entry occurs normally in p125(FAK)-deficient fibroblasts. We now provide evidence that Ad internalization, a process which is mediated by LY,integrins, also requires p130(CAS) and phosphatidylinositol-3-OH kinase (PI 3-kinase). Ad induces p130(CAS) phosphorylation and inhibition of p130(CAS) phosphorylation by tyrphostin and genistein, or expression of the substrate domain deleted p130(CAS) blocks Ad internalization. p130(CAS) was also found to associate with the p85 subunit of PI 3-kinase through its proline-rich domain during virus internalization and expression of p130(CAS) containing a deleted proline-rich domain (PRD) inhibited adenovirus cell entry. We showed further that the RPLPSPP motif in the proline-richregion of p130(CAS) interacts with the SH3 domain of p85/PI 3-kinase. These studies reveal the molecular basis by which p130(CAS) coordinates the signaling pathways involved in integrin-mediated Ad endocytosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 20:49:33