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Titolo:
HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2
Autore:
Metzler, M; Legendre-Guillemin, V; Gan, L; Chopra, V; Kwok, A; McPherson, PS; Hayden, MR;
Indirizzi:
Univ British Columbia, Dept Med Genet, Ctr Mol Med & Therapeut, Vancouver,BC V5Z 4H4, Canada Univ British Columbia Vancouver BC Canada V5Z 4H4 uver,BC V5Z 4H4, Canada McGill Univ, Montreal Neurol Inst, Dept Neurol & Neurosurg, Montreal, PQ H3A 2B4, Canada McGill Univ Montreal PQ Canada H3A 2B4 surg, Montreal, PQ H3A 2B4, Canada
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 42, volume: 276, anno: 2001,
pagine: 39271 - 39276
SICI:
0021-9258(20011019)276:42<39271:HFICET>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYNAPTIC VESICLE ENDOCYTOSIS; SACCHAROMYCES-CEREVISIAE; INTERACTING PROTEIN; SPLICE VARIANTS; COATED PITS; HUNTINGTIN; DOMAIN; COMPONENTS; FAMILY; SITES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Hayden, MR Univ British Columbia, Dept Med Genet, Ctr Mol Med & Therapeut,980 W 28thAve, Vancouver, BC V5Z 4H4, Canada Univ British Columbia 980 W 28th Ave Vancouver BC Canada V5Z 4H4
Citazione:
M. Metzler et al., "HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2", J BIOL CHEM, 276(42), 2001, pp. 39271-39276

Abstract

Polyglutamine expansion in huntingtin is the underlying mutation leading to neurodegeneration in Huntington disease. This mutation influences the interaction of huntingtin with different proteins, including huntingtin-interacting protein I (HIP(), in which affinity to bind to mutant huntingtin is profoundly reduced. Here we demonstrate that HIP( colocalizes with markers of clathrin-mediated endocytosis in neuronal cells and is highly enriched onclathrin-coated vesicles (CCVs) purified from brain homogenates. HIP( binds to the clathrin adaptor protein 2 (AP2) and the terminal domain of the clathrin heavy chain, predominantly through a small fragment encompassing amino acids 276-335. This region, which contains consensus clathrin- and AP2-binding sites, functions in conjunction with the coiled-coil domain to target HIP( to CCVs. Expression of various HIP1 fragments leads to a potent block of clathrin-mediated endocytosis. Our findings demonstrate that HIP1 is anovel component of the endocytic machinery.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/06/20 alle ore 01:43:56