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Titolo:
Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis
Autore:
Confalonieri, S; Salcini, AE; Puri, C; Tacchetti, C; Di Fiore, PP;
Indirizzi:
Ist Europeo Oncol, Dept Expt Oncol, I-20141 Milan, Italy Ist Europeo Oncol Milan Italy I-20141 t Expt Oncol, I-20141 Milan, Italy Univ Genoa, Dept Expt Med, Anat Sect, I-16132 Genoa, Italy Univ Genoa Genoa Italy I-16132 Expt Med, Anat Sect, I-16132 Genoa, Italy FIRC Inst Mol Oncol, IFOM, I-20139 Milan, Italy FIRC Inst Mol Oncol Milan Italy I-20139 ncol, IFOM, I-20139 Milan, Italy
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 4, volume: 150, anno: 2000,
pagine: 905 - 911
SICI:
0021-9525(20000821)150:4<905:TPOEIR>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMAL GROWTH-FACTOR; RECEPTOR-MEDIATED ENDOCYTOSIS; KINASE SUBSTRATE; PLASMA-MEMBRANE; CLATHRIN COATS; EH-DOMAIN; TRANSFERRIN; BINDING; AP-2; ASSOCIATION;
Keywords:
Eps15; phosphotyrosine; endocytosis; epidermal growth factor receptor; transferrin receptor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Di Fiore, PP Ist Europeo Oncol, Dept Expt Oncol, Via Ripamonti 435, I-20141 Milan, Italy Ist Europeo Oncol Via Ripamonti 435 Milan Italy I-20141 taly
Citazione:
S. Confalonieri et al., "Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis", J CELL BIOL, 150(4), 2000, pp. 905-911

Abstract

Membrane receptors are internalized either constitutively or upon ligand engagement,Whereas there is evidence for differential regulation of the two processes, little is known about the molecular machinery involved. Previousstudies have shown that an unidentified kinase substrate is required for endocytosis of the epidermal growth factor receptor (EGFR), the prototypicalligand-inducible receptor, but not of the transferrin receptor (TfR), the prototypical constitutively internalized receptor, Eps15, an endocytic protein that is tyrosine phosphorylated by EGFR, is a candidate for such a function. Here, we show that tyrosine phosphorylation of Eps15 is necessary forinternalization of the EGFR, but not of the TfR. We mapped Tyr 850 as the major in vivo tyrosine phosphorylation site of Eps15. A phosphorylation-negative mutant of Eps15 acted as a dominant negative on the internalization of the EGFR, but not of the TfR. A phosphopeptide, corresponding to the phosphorylated sequence of Eps15, inhibited EGFR endocytosis, suggesting that phosphotyrosine in Eps15 serves as a docking site for a phosphotyrosine binding protein. Thus, tyrosine phosphorylation of Eps15 represents the first molecular determinant, other than those contained in the receptors themselves, which is involved in the differential regulation of constitutive vs. regulated endocytosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 10:26:37