Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Topological restriction of SNARE-dependent membrane fusion
Autore:
Parlati, F; McNew, JA; Fukuda, R; Miller, R; Sollner, TH; Rothman, JE;
Indirizzi:
Mem Sloan Kettering Canc Ctr, Cellular Biochem & Biophys Program, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 New York, NY 10021 USA
Titolo Testata:
NATURE
fascicolo: 6801, volume: 407, anno: 2000,
pagine: 194 - 198
SICI:
0028-0836(20000914)407:6801<194:TROSMF>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST SECRETORY PATHWAY; GOLGI-COMPLEX; V-SNARE; ENDOPLASMIC-RETICULUM; VESICULAR TRANSPORT; PROTEIN; VESICLES; IDENTIFICATION; ACTIVATION; ENCODES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Rothman, JE Mem Sloan Kettering Canc Ctr, Cellular Biochem & Biophys Program, 1275 York Ave,Box 251, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr 1275 York Ave,Box 251 New York NY USA 10021
Citazione:
F. Parlati et al., "Topological restriction of SNARE-dependent membrane fusion", NATURE, 407(6801), 2000, pp. 194-198

Abstract

To fuse transport vesicles with target membranes, proteins of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) complex must be located on both the vesicle (v-SNARE) and the target membrane (t-SNARE)(1). In yeast, four integral membrane proteins, Sed5, Bos1, Sec22 and Bet1 (refs 2-6), each probably contribute a single helix to form the SNARE complex that is needed for transport from endoplasmic reticulum to Golgi(7-11). This generates a four-helix bundle(12), which ultimately mediates the actual fusion event(13). Here we explore how the anchoring arrangement of the four helices affects their ability to mediate fusion. We reconstituted two populations of phospholipid bilayer vesicles, with the individual SNARE proteins distributed in all possible combinations between them. Of the eight non-redundant permutations of four subunits distributed over two vesicle populations, only one results in membrane fusion. Fusion only occurs when the v-SNARE Bet1 is on one membrane and the syntaxin heavy chain Sed5 andits two light chains, Bos1 and Sec22, are on the other membrane where theyform a functional t-SNARE. Thus, each SNARE protein is topologically restricted by design to function either as a v-SNARE or as part of a t-SNARE complex.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/01/21 alle ore 22:47:55