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Titolo:
STOICHIOMETRIC INTERACTION OF THE EPIDERMAL GROWTH-FACTOR RECEPTOR WITH THE CLATHRIN-ASSOCIATED PROTEIN COMPLEX AP-2
Autore:
SORKIN A; MCKINSEY T; SHIH W; KIRCHHAUSEN T; CARPENTER G;
Indirizzi:
UNIV COLORADO,HLTH SCI CTR,DEPT PHARMACOL,4200 E 9TH AVE DENVER CO 80262 VANDERBILT UNIV,SCH MED,DEPT BIOCHEM NASHVILLE TN 37232 HARVARD UNIV,SCH MED,DEPT CELL BIOL BOSTON MA 02115 CTR BLOOD RES BOSTON MA 02115
Titolo Testata:
The Journal of biological chemistry
fascicolo: 2, volume: 270, anno: 1995,
pagine: 619 - 625
SICI:
0021-9258(1995)270:2<619:SIOTEG>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGAND-INDUCED INTERNALIZATION; COATED VESICLE PROTEINS; AMINO-ACID SEQUENCE; PLASMA-MEMBRANE; MEDIATED ENDOCYTOSIS; ADAPTER PROTEIN; INVITRO BINDING; KINASE-ACTIVITY; PITS; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
A. Sorkin et al., "STOICHIOMETRIC INTERACTION OF THE EPIDERMAL GROWTH-FACTOR RECEPTOR WITH THE CLATHRIN-ASSOCIATED PROTEIN COMPLEX AP-2", The Journal of biological chemistry, 270(2), 1995, pp. 619-625

Abstract

Plasma membrane clathrin-associated protein complexes (AP-2) have been shown to co-immunoprecipitate with the epidermal growth factor (EGF)receptor (Sorkin A., and Carpenter, G. (1993) Science 261, 612-615). Hence, we analyzed the stoichiometry of the EGF receptor interaction with AP-2 using a new antibody that efficiently immunoprecipitates native AP-2. EGF receptor AP-2 complexes were isolated from S-35-labeled cells treated with EGF by EGF receptor affinity chroma tography followed by precipitation with the antibody to AP-2. Quantitation of the relative molar concentrations of the proteins found in the complex revealed that 1 mol of AP-2 was associated with approximately 1.1 mol of EGF receptor. No other proteins were present in significant molar concentrations relative to AP-2. indicating that other proteins are not stoichiometrically involved in the interaction of EGF receptors and AP-2 in vitro. Co-immunoprecipitation experiments in cells expressing a mutantEGF receptor demonstrated that the cyto plasmic carboxyl-terminal 214residues of the EGF receptor are essential for interaction with AP-2.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 02:25:53