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Titolo:
VAP-A binds promiscuously to both v- and tSNAREs
Autore:
Weir, ML; Xie, H; Klip, A; Trimble, WS;
Indirizzi:
Hosp Sick Children, Cell Biol Programme, Toronto, ON M5G 1X8, Canada Hosp Sick Children Toronto ON Canada M5G 1X8 Toronto, ON M5G 1X8, Canada Univ Toronto, Dept Biochem, Toronto, ON M5G 1X8, Canada Univ Toronto Toronto ON Canada M5G 1X8 ochem, Toronto, ON M5G 1X8, Canada
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 3, volume: 286, anno: 2001,
pagine: 616 - 621
SICI:
0006-291X(20010824)286:3<616:VBPTBV>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOPLASMIC-RETICULUM; PROTEIN-TRANSPORT; GOLGI-APPARATUS; MEMBRANE-FUSION; ANGSTROM RESOLUTION; VESICULAR TRANSPORT; MOLECULAR-CLONING; CRYSTAL-STRUCTURE; ASCARIS-SUUM; SNARE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Trimble, WS Hosp Sick Children, Cell Biol Programme, 555 Univ Ave, Toronto, ON M5G 1X8, Canada Hosp Sick Children 555 Univ Ave Toronto ON Canada M5G 1X8 nada
Citazione:
M.L. Weir et al., "VAP-A binds promiscuously to both v- and tSNAREs", BIOC BIOP R, 286(3), 2001, pp. 616-621

Abstract

Proteins that bind to SNAREs may regulate their function. One such protein, VAP-33, was first discovered in Aplysia californica and has two mammalianhomologues, VAP-A and VAP-B. VAP-A has been implicated in vesicle targeting to the plasma membrane based on its location in polarized cells and its ability to bind VAMP in vitro. Here, we demonstrate that VAP-A is a widely expressed resident of the ER/Golgi intermediate compartment in COS-7 cells. Moreover, we demonstrate that VAM-P-binding and VAP-dimerization require both the N- and C-terminal domains of VAP-A and also that VAP-A binds to a wide range of SNAREs and fusion-related proteins including syntaxin 1A, rbet1, rsec22, alpha SNAP, and NSF. Together, these results suggest that VAP-A is not a regulator of a specific VAMP, but rather may play a more general role in SNARE-mediated vesicle traffic between the ER and Golgi in nonpolarized cells. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/01/21 alle ore 03:54:02