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Titolo:
Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis
Autore:
Wendland, B; Steece, KE; Emr, SD;
Indirizzi:
Johns Hopkins Univ, Dept Biol, Baltimore, MD 21218 USA Johns Hopkins UnivBaltimore MD USA 21218 t Biol, Baltimore, MD 21218 USA Univ Calif San Diego, Div Cellular & Mol Med, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 ol Med, La Jolla, CA 92093 USA Univ Calif San Diego, Howard Hughes Med Inst, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 d Inst, La Jolla, CA 92093 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 16, volume: 18, anno: 1999,
pagine: 4383 - 4393
SICI:
0261-4189(19990816)18:16<4383:YECAEN>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE KINASE SUBSTRATE; AP-3 ADAPTER COMPLEX; EH-DOMAIN; ARRESTIN/CLATHRIN INTERACTION; MEDIATED ENDOCYTOSIS; ACTIN CYTOSKELETON; NERVE-TERMINALS; EPS15 HOMOLOGY; PROTEIN; INTERNALIZATION;
Keywords:
actin; clathrin; endocytosis; ENTH domain; epsin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Wendland, B Johns Hopkins Univ, Dept Biol, Baltimore, MD 21218 USA Johns Hopkins Univ Baltimore MD USA 21218 imore, MD 21218 USA
Citazione:
B. Wendland et al., "Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis", EMBO J, 18(16), 1999, pp. 4383-4393

Abstract

The mammalian protein epsin is required for endocytosis, In this study, wehave characterized two homologous yeast proteins, Ent1p and Ent2p, which are similar to mammalian epsin. An essential function for the highly conserved N-terminal epsin N-terminal homology (ENTH) domain was revealed using deletions and randomly generated temperature-sensitive ent1 alleles, Changes in conserved ENTH domain residues in ent1(ts) cells revealed defects in endocytosis and actin cytoskeleton structure. The Ent1 protein was localized to peripheral and internal punctate structures, and biochemical fractionation studies found the protein associated with a large, Triton X-100-insolublepellet. Finally, an Ent1p clathrin-binding domain was mapped to the final eight amino acids (RGYTLIDL*) in the Ent1 protein sequence. Based on these and other data, we propose that the yeast epsin-like proteins are essentialcomponents of an endocytic complex that may act at multiple stages in the endocytic pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 13:45:35