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Titolo:
Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis
Autore:
Morinaka, K; Koyama, S; Nakashima, S; Hinoi, T; Okawa, K; Iwamatsu, A; Kikuchi, A;
Indirizzi:
Hiroshima Univ, Sch Med, Dept Biochem, Minami Ku, Hiroshima 7348551, JapanHiroshima Univ Hiroshima Japan 7348551 nami Ku, Hiroshima 7348551, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan 2360004 agawa 2360004, Japan
Titolo Testata:
ONCOGENE
fascicolo: 43, volume: 18, anno: 1999,
pagine: 5915 - 5922
SICI:
0950-9232(19991021)18:43<5915:EBTTED>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE DISSOCIATION STIMULATOR; TYROSINE KINASE SUBSTRATE; RAS-INDUCED TRANSFORMATION; INSULIN-RECEPTOR; SACCHAROMYCES-CEREVISIAE; SIGNAL-TRANSDUCTION; ACTIN CYTOSKELETON; NERVE-TERMINALS; EPS15 HOMOLOGY; DUAL ROLE;
Keywords:
Epsin; POB1; EH domain; endocytosis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Kikuchi, A Hiroshima Univ, Sch Med, Dept Biochem, Minami Ku, 1-2-3 Kasumi,Hiroshima 7348551, Japan Hiroshima Univ 1-2-3 Kasumi Hiroshima Japan 7348551 551, Japan
Citazione:
K. Morinaka et al., "Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis", ONCOGENE, 18(43), 1999, pp. 5915-5922

Abstract

POB1 has been identified as a RalBP1-binding protein and has the Eps15 homology (EH) domain. The EH domain-containing proteins have been suggested tobe involved in clathrin-dependent endocytosis. To clarify the function of POB1, we purified a protein which binds to the EH domain of POB1 from bovine brain cytosol and identified it as Epsin, which is known to bind to the EH domain of Eps15. Epsin has three Asn-Pro-Phe (NPF) motifs in the C-terminal region, which are known to form the core sequence for the binding to theEH domain. The EH domain of POB1 interacted directly with the region containing the NPF motifs of Epsin. Expression of Epsin in CHO-IR cells inhibited internalization of insulin although it affected neither insulin-binding nor autophosphorylation activities of the insulin receptor. Taken together with the observations that Epsin is involved in internalization of the receptors for epidermal growth factor and transferrin, these results suggest that Epsin is a binding partner of POB1 and their binding regulates receptor-mediated endocytosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/01/21 alle ore 04:20:50