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Titolo:
Numb is an endocytic protein
Autore:
Santolini, E; Puri, C; Salcini, AE; Gagliani, MC; Pelicci, PG; 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, Anat Sect, Dept Expt Med, I-16132 Genoa, Italy Univ Genoa Genoa Italy I-16132 Sect, Dept Expt Med, I-16132 Genoa, Italy IFOM, FIRC Inst Mol Oncol, I-20134 Milan, Italy IFOM Milan Italy I-20134IFOM, FIRC Inst Mol Oncol, I-20134 Milan, Italy
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 6, volume: 151, anno: 2000,
pagine: 1345 - 1351
SICI:
0021-9525(200012)151:6<1345:NIAEP>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE KINASE SUBSTRATE; MOUSE CORTICAL NEUROGENESIS; MAMMALIAN NUMB; CELL FATE; ASYMMETRIC LOCALIZATION; PLASMA-MEMBRANE; EPS15; NOTCH; BINDING; DOMAIN;
Keywords:
numb; endocytosis; EH domain; EGFR; Eps15;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
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:
E. Santolini et al., "Numb is an endocytic protein", J CELL BIOL, 151(6), 2000, pp. 1345-1351

Abstract

Numb is a protein that in Drosophila determines cell fate as a result of its asymmetric partitioning at mitosis. The function of Numb has been linkedto its ability to bind and to biologically antagonize Notch, a membrane receptor that also specifies cell fate. The biochemical mechanisms underlyingthe action of Numb, however, are still largely unknown. The wide pattern of expression of Numb suggests a general function in cellular homeostasis that could be additional to, or part of, its action in fate determination. Such a function could be endocytosis, as suggested by the interaction of Numbwith Eps15, a component of the endocytic machinery. Here, we demonstrate that Numb is an endocytic protein. We found that Numb localizes to endocyticorganelles and is cotrafficked with internalizing receptors. Moreover, it associates with the appendage domain of alpha adaptin, a subunit of AP2, a major component of clathrin-coated pits. Finally, fragments of Numb act as dominant negatives on both constitutive and ligand-regulated receptor-mediated internalization, suggesting a general role for Numb in the endocytic process.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 23:54:18