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Titolo:
EPIDERMAL GROWTH-FACTOR RECEPTOR INTERACTION WITH CLATHRIN ADAPTERS IS MEDIATED BY THE TYR(974)-CONTAINING INTERNALIZATION MOTIF
Autore:
SORKIN A; MAZZOTTI M; SORKINA T; SCOTTO L; BEGUINOT L;
Indirizzi:
UNIV COLORADO,HLTH SCI CTR,DEPT PHARMACOL,4200 E 9TH AVE DENVER CO 80262 HOSP SAN RAFFAELE,MOLEC ONCOL LAB,DIBIT I-20132 MILAN ITALY HOSP SAN RAFFAELE,CNR,INST NEUROSCI & BIOMMAGINI I-20132 MILAN ITALY
Titolo Testata:
The Journal of biological chemistry
fascicolo: 23, volume: 271, anno: 1996,
pagine: 13377 - 13384
SICI:
0021-9258(1996)271:23<13377:EGRIWC>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
LYSOSOMAL ACID-PHOSPHATASE; LIGAND-INDUCED INTERNALIZATION; HUMAN-FIBROBLASTS; DOWN-REGULATION; COATED PITS; ENDOCYTIC SYSTEM; INVITRO BINDING; KINASE-ACTIVITY; EGF RECEPTOR; DEGRADATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
49
Recensione:
Indirizzi per estratti:
Citazione:
A. Sorkin et al., "EPIDERMAL GROWTH-FACTOR RECEPTOR INTERACTION WITH CLATHRIN ADAPTERS IS MEDIATED BY THE TYR(974)-CONTAINING INTERNALIZATION MOTIF", The Journal of biological chemistry, 271(23), 1996, pp. 13377-13384

Abstract

The carboxyl-terminal regulatory domain of the epidermal growth factor (EGF) receptor is essential for its endocytosis and interaction withthe clathrin-associated protein complex AP-2. To identify AP-2 binding motif in the receptor, several single and multiple-point mutations within the region between residues 966 and 977 of the human EGF receptor were made, and the mutant receptors were expressed in NIH3T3 cells. Mutation of tyrosine 974 alone or together with surrounding residues and the deletion of residues 973-975 essentially eliminated AP-2 co-immunoprecipitation with the EGF receptor, Furthermore, a synthetic peptide corresponding to receptor residues 964-978 blocked AP-2 associationwith the wild-type EGF receptor, These data suggest that AP-2 has only one high-affinity binding site in the EGF receptor composed of Tyr(974)-containing motif. Receptor mutants that did not bind AP-2 displayed a lower rate of internalization, down-regulation, and turnover compared to wild type receptors when expressed at high levels. However, similar receptor mutants expressed at low levels were internalized and down-regulated as efficiently as wild type receptors, Internalization ofthe mutant receptors lacking the high-affinity binding site for AP-2 was inhibited by K+-depletion of the cells, indicating that their endocytosis required intact coated pits, We suggest that whereas one mechanism of EGF receptor recruitment into coated pits involves high-affinity binding of AP-2 to Tyr(974)-containing motif, another pathway may be mediated by weak receptor/AP-2 interactions or by proteins other than AP-2.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 01:08:47