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Titolo:
Tyrosine phosphorylation of C-Cbl facilitates adhesion and spreading whilesuppressing anchorage-independent growth of V-Abl-transformed NIH3T3 fibroblasts
Autore:
Feshchenko, EA; Shore, SK; Tsygankov, AY;
Indirizzi:
Temple Univ, Sch Med, Dept Immunol & Microbiol, Philadelphia, PA 19140 USATemple Univ Philadelphia PA USA 19140 crobiol, Philadelphia, PA 19140 USA Temple Univ, Sch Med, Fels Inst Canc Res & Mol Biol, Philadelphia, PA 19140 USA Temple Univ Philadelphia PA USA 19140 ol Biol, Philadelphia, PA 19140 USA
Titolo Testata:
ONCOGENE
fascicolo: 25, volume: 18, anno: 1999,
pagine: 3703 - 3715
SICI:
0950-9232(19990624)18:25<3703:TPOCFA>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL ANTIGEN RECEPTOR; PROTOONCOGENE PRODUCT P120(CBL); PHOSPHOTYROSINE-BINDING DOMAIN; PHOSPHOINOSITIDE 3-OH KINASE; INTEGRIN SIGNALING PATHWAY; SRC HOMOLOGY-3 DOMAIN; CRK ADAPTER PROTEINS; ACTIVATED T-CELLS; PHOSPHATIDYLINOSITOL 3-KINASE; EGF RECEPTOR;
Keywords:
Abl; Cbl; adhesion; morphology; transformation; tyrosine phosphorylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
85
Recensione:
Indirizzi per estratti:
Indirizzo: Tsygankov, AY Temple Univ, Sch Med, Dept Immunol & Microbiol, 3400 Broad St, Philadelphia, PA 19140 USA Temple Univ 3400 Broad St Philadelphia PA USA19140 9140 USA
Citazione:
E.A. Feshchenko et al., "Tyrosine phosphorylation of C-Cbl facilitates adhesion and spreading whilesuppressing anchorage-independent growth of V-Abl-transformed NIH3T3 fibroblasts", ONCOGENE, 18(25), 1999, pp. 3703-3715

Abstract

The protooncogenic protein c-Cbl becomes tyrosine phosphorylated in normalcells in response to a variety of external stimuli, as well as in cells transformed by oncogenic protein tyrosine kinases. Tyrosine phosphorylation of c-Cbl upregulates its binding to multiple crucial signaling molecules. However, the biological consequences of c-Cbl-mediated signaling are insufficiently understood. To analyse the biological functions of c-Cbl, we overexpressed wild-type c-Cbl and its tyrosine phosphorylation-defective mutant form in v-Abl-transformed NIH3T3 fibroblasts. In this system, wild-type c-Cblfacilitated adhesion and spreading of v-Abl-transformed fibroblasts on theextracellular matrix, while reducing anchorage independence of these cells, as measured by their colony-forming efficiency in soft agar. Therefore, overexpression of wild-type c-Cbl exhibits an overall transformation-suppressing effect. By contrast, overexpression of a tyrosine phosphorylation-defective form of c-Cbl increases neither adhesion nor anchorage dependence of v-Abl-transformed fibroblasts. Analysis of the role of individual tyrosine phosphorylation sites of c-Cbl in these phenomena indicates that both phosphatidylinositol-3' kinase and the CrkL adaptor protein may be involved in the observed effects of c-Cbl. To summarize, the results presented in this report indicate that c-Cbl is involved in regulation of cell adhesion and cytoskeletal rearrangements, and that these effects of c-Cbl are dependent onits tyrosine phosphorylation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 06:11:17