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Titolo:
THE E-CADHERIN COMPLEX CONTAINS THE SRC SUBSTRATE P120
Autore:
AGHIB DF; MCCREA PD;
Indirizzi:
UNIV CALIF SAN FRANCISCO,DEPT GROWTH & DEV SAN FRANCISCO CA 94143 UNIV TEXAS,MD ANDERSON CANC CTR,DEPT BIOCHEM & MOLEC BIOL 117 HOUSTONTX 77030
Titolo Testata:
Experimental cell research
fascicolo: 1, volume: 218, anno: 1995,
pagine: 359 - 369
SICI:
0014-4827(1995)218:1<359:TECCTS>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-CELL-ADHESION; POLARITY GENE ARMADILLO; UVOMORULIN-CATENIN COMPLEX; ADHERENS-TYPE JUNCTIONS; MOLECULE E-CADHERIN; ROUS-SARCOMA VIRUS; BETA-CATENIN; TYROSINE PHOSPHORYLATION; EPITHELIAL-CELLS; XENOPUS EMBRYOS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
87
Recensione:
Indirizzi per estratti:
Citazione:
D.F. Aghib e P.D. Mccrea, "THE E-CADHERIN COMPLEX CONTAINS THE SRC SUBSTRATE P120", Experimental cell research, 218(1), 1995, pp. 359-369

Abstract

Using normal MDCK cells, and MDCK cells stably transfected with a temperature-sensitive viral src allele (pp60 ts-v-src), we have examined the composition and tyrosine phosphorylation of the E-cadherin complex, E-cadherin is a transmembrane calcium-dependent cell-cell adhesion molecule that is complexed with cytoplasmic proteins including alpha-catenin, beta-catenin, plakoglobin (gamma-catenin), and actin. We have identified two heterodimeric complexes which demonstrate that alpha-catenin interacts directly with beta-catenin, or with plakoglobin, in theabsence of E-cadherin. beta-Catenin has previously been shown to binddirectly to E-cadherin. We propose that E-cadherin associates with alpha-catenin, and thereby the actin cytoskeleton, via either beta-catenin or plakoglobin. We have further identified three new but related protein components of the E-cadherin complex, which are each cross-reactive by Western blot analysis to antibodies directed against p120, a phosphotyrosine substrate of src, and a phosphotyrosine, phosphoserine, and phosphothreonine substrate of growth factor-stimulated signaling pathways. Greater quantities of the p120-related proteins were found present in the E-cadherin immunoprecipitates of ts-src MDCK cells compared to normal MDCK cells, while two of the p120 cross-reactive species were significantly tyrosine phosphorylated in both normal and ts-src MDCK cells. The association of p120-related species with the E-cadherincomplex adds them to our consideration of possible modulators of cadherin function. Likewise, the newly identified alpha-catenin-beta-catenin and alpha-catenin-plakoglobin dimers may have interesting biological properties, conceivably including the titration of catenins between cadherin and APC complexes. (C) 1995 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/08/20 alle ore 14:38:24