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Titolo:
Identification of Rab6 as an N-ethylmaleimide-sensitive fusion protein-binding protein
Autore:
Han, SY; Park, DY; Park, SD; Hong, SH;
Indirizzi:
Seoul Natl Univ, Inst Mol Biol & Genet, Seoul 151742, South Korea Seoul Natl Univ Seoul South Korea 151742 enet, Seoul 151742, South Korea Seoul Natl Univ, Sch Biol Sci, Seoul 151742, South Korea Seoul Natl Univ Seoul South Korea 151742 Sci, Seoul 151742, South Korea
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 352, anno: 2000,
parte:, 1
pagine: 165 - 173
SICI:
0264-6021(20001115)352:<165:IORAAN>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
MEMBRANE-FUSION; VESICULAR TRANSPORT; GOLGI PROTEINS; IN-VITRO; NSF; SNAP; VESICLES; RELEASE; DOMAIN; FAMILY;
Keywords:
NSF; Rab protein; small G-protein; vesicular transport;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Hong, SH Seoul Natl Univ, Inst Mol Biol & Genet, Seoul 151742, South KoreaSeoul Natl Univ Seoul South Korea 151742 ul 151742, South Korea
Citazione:
S.Y. Han et al., "Identification of Rab6 as an N-ethylmaleimide-sensitive fusion protein-binding protein", BIOCHEM J, 352, 2000, pp. 165-173

Abstract

In this study we show the interaction of N-ethylmaleimide-sensitive fusionprotein (NSF) with a small GT:P-binding protein, Rab6. NSF is an ATPase involved in the vesicular transport within eukaryotic cells. Using the yeast two-hybrid system, we have isolated new NSF-binding proteins from the rat lung cDNA library. One of them was Rab6, which is invoked in the vesicular transport within the Golgi and trans-Golgi network as a Ras-like GTPase, We demonstrated that the N-terminal domain of NSF interacted with the C-terminal domain of Rab6, and these proteins were co-immunoprecipitated from the rat brain extract. This interaction was maintained preferentially in the presence of hydrolysable ATP. Recombinant NSF-His(6) can also bind to C-terminal Rab6-glutathione S-transferase under the conditions to allow the ATP hydrolysis. Surprisingly, Rab6 stimulates the ATPase activity of NSF by approx. 2-fold as does alpha -soluble NSF attachment protein receptor. Anti-Rab6 polyclonal antibodies significantly inhibited the Rab6-stimulated ATPase activity of NSF. Furthermore, we found that Rab3 and Rab4 can also associate with NSF and stimulate its ATPase activity. Taken together, we propose a model in which Rab can form an ATP hydrolysis-regulated complex with NSF, andfunction as a signalling molecule to deliver the signal of vesicle fusion through the interaction with NSF.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 17/01/21 alle ore 18:01:53