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Titolo:
THE TYROSINE KINASE SUBSTRATE EPS15 IS CONSTITUTIVELY ASSOCIATED WITHTHE PLASMA-MEMBRANE ADAPTER AP-2
Autore:
BENMERAH A; GAGNON J; BEGUE B; MEGARBANE B; DAUTRYVARSAT A; CERFBENSUSSAN N;
Indirizzi:
HOP NECKER ENFANTS MALAD,INSERM,U429,149 RUE SEVRES F-75743 PARIS 15 FRANCE HOP NECKER ENFANTS MALAD,INSERM,U429 F-75743 PARIS 15 FRANCE INST BIOL STRUCT GRENOBLE FRANCE INST PASTEUR,CNRS,URA 1960,UNITE BIOL INTERACT CELLULAIRES PARIS FRANCE
Titolo Testata:
The Journal of cell biology
fascicolo: 6, volume: 131, anno: 1995,
parte:, 2
pagine: 1831 - 1838
SICI:
0021-9525(1995)131:6<1831:TTKSEI>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLATHRIN-COATED VESICLES; EPIDERMAL GROWTH-FACTOR; INTESTINAL LYMPHOCYTES; PROTEIN COMPLEX; GOLGI-APPARATUS; INVITRO BINDING; CLONING; RECEPTORS; SUBUNIT; CHAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
A. Benmerah et al., "THE TYROSINE KINASE SUBSTRATE EPS15 IS CONSTITUTIVELY ASSOCIATED WITHTHE PLASMA-MEMBRANE ADAPTER AP-2", The Journal of cell biology, 131(6), 1995, pp. 1831-1838

Abstract

The ubiquitous eps15 protein was initially described as a substrate of the EGF receptor kinase. Its functions are not yet delineated and this work provides evidence for its possible role in endocytosis. A novel anti-eps15 antibody, 6G4, coimmunoprecipitated proteins of molecularmass 102 kD. In human cells, these proteins were identified as the alpha- and beta-adaptins of the AP-2 complex on the basis of their NH2-terminal sequence and their immunoreactivity with anti-alpha- and anti-beta-adaptin antibodies but not with anti-gamma-adaptin antibody. In addition, the anti-eps15 antibody coimmunoprecipitated metabolically labeled polypeptides with molecular mass of 50 and 17 kD, comparable to those of the two other components of the AP-2 complex, mu 2 and sigma 2. Constitutive association of eps15 with AP-2 was confirmed by two sets of experiments, First, eps15 was detected in immunoprecipitates of anti-alpha- and anti-beta-adaptin antibodies. Second, alpha- and beta-but not gamma-adaptins were precipitated by a glutathione-S-transferase eps15 fusion protein. The association of eps15 with AP-2 was ubiquitous and conserved between species, since it was observed in human lymphocytes and epithelial cells and in murine NIH3T3 fibroblasts. Our results are in keeping with a recent study showing homology between the NH2-terminal domains of eps15 and the product of the gene END3, involved in clathrin-mediated endocytosis of the pheromone alpha factor in Saccharomyces cerevisiae, and suggest a possible role for eps15 in clathrin-mediated endocytosis in mammals.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 20:54:50