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Titolo:
Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors
Autore:
Nakashima, S; Morinaka, K; Koyama, S; Ikeda, M; Kishida, M; Okawa, K; Iwamatsu, A; Kishida, S; 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:
EMBO JOURNAL
fascicolo: 13, volume: 18, anno: 1999,
pagine: 3629 - 3642
SICI:
0261-4189(19990701)18:13<3629:SGPRAI>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
GDP DISSOCIATION STIMULATOR; TYROSINE KINASE SUBSTRATE; PUTATIVE EFFECTOR PROTEIN; EH-DOMAIN; POSTTRANSLATIONAL MODIFICATIONS; INDUCED TRANSFORMATION; MEDIATED ENDOCYTOSIS; BINDING PROTEIN-1; EUKARYOTIC CELLS; AMINO-ACID;
Keywords:
endocytosis; epsin; POB1; Ral; RalBP1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
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:
S. Nakashima et al., "Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors", EMBO J, 18(13), 1999, pp. 3629-3642

Abstract

The involvement of Ral and its downstream molecules in receptor-mediated endocytosis was examined. Expression of either Ral(G23V) or Ral(S28N), whichare known to be constitutively active and dominant-negative forms, respectively, in A431 cells blocked internalization of epidermal growth factor (EGF), Stable expression of Ral(G23V) or RalS28N in CHO-IR cells also inhibited internalization of insulin. Internalization of EGF and insulin was not affected by full-length RalBP1 which is an effector protein of Ral, but was inhibited by its C-terminal region which binds directly to Ral and POB1. POB1 is a binding protein of RalBP1 and has the Eps15 homology (EH) domain, Deletion mutants of POB1 inhibited internalization of EGF and insulin. However, internalization of transferrin was unaffected by Ral, RalBP1, POB1 and their mutants. Epsin and Eps15 have been reported to be involved in the regulation of endocytosis of the receptors for EGF and transferrin. The EH domain of POB1 bound directly to Epsin and Eps15. Taken together with the observation that EGF and insulin activate Ral, these results suggest that Ral, RalBP1 and POB1 transmit the signal from the receptors to Epsin and Eps15, thereby regulating ligand-dependent receptor-mediated endocytosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 09:18:47