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Titolo:
Botulinum neurotoxin E-insensitive mutants of SNAP-25 fail to bind VAMP but support exocytosis
Autore:
Washbourne, P; Bortoletto, N; Graham, ME; Wilson, MC; Burgoyne, RD; Montecucco, C;
Indirizzi:
Univ New Mexico, Dept Neurosci, Albuquerque, NM 87131 USA Univ New MexicoAlbuquerque NM USA 87131 rosci, Albuquerque, NM 87131 USA Univ Padua, CNR, Ctr Biomembrane, Padua, Italy Univ Padua Padua ItalyUniv Padua, CNR, Ctr Biomembrane, Padua, Italy Univ Padua, Dept Biomed Sci, Padua, Italy Univ Padua Padua ItalyUniv Padua, Dept Biomed Sci, Padua, Italy Univ Liverpool, Physiol Lab, Liverpool L69 3BX, Merseyside, England Univ Liverpool Liverpool Merseyside England L69 3BX , Merseyside, England
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 6, volume: 73, anno: 1999,
pagine: 2424 - 2433
SICI:
0022-3042(199912)73:6<2424:BNEMOS>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
PERMEABILIZED CHROMAFFIN CELLS; SNARE COMPLEX; NEUROTRANSMITTER RELEASE; CA2+-DEPENDENT EXOCYTOSIS; CLOSTRIDIAL NEUROTOXINS; CRYSTAL-STRUCTURE; PLASMA-MEMBRANE; VESICLE FUSION; TETANUS TOXIN; CDNA CLONES;
Keywords:
SNAP-25; syntaxin; vesicle-associated membrane protein; SNAP receptor; botulinum neurotoxin; exocytosis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Washbourne, P Univ New Mexico, Dept Neurosci, Basic Med Sci Bldg,915 Camino Salud, Albuquerque, NM 87131 USA Univ New Mexico Basic Med Sci Bldg,915 Camino Salud Albuquerque NM USA 87131
Citazione:
P. Washbourne et al., "Botulinum neurotoxin E-insensitive mutants of SNAP-25 fail to bind VAMP but support exocytosis", J NEUROCHEM, 73(6), 1999, pp. 2424-2433

Abstract

Neurotransmitter release from synaptic vesicles is mediated by complex machinery, which includes the v- and t-SNAP receptors (SNAREs), vesicle-associated membrane protein (VAMP), synaptotagmin, syntaxin, and synaptosome-associated protein of 25 kDa (SNAP;25). They are essential for neurotransmitterexocytosis because they are the proteolytic substrates of the clostridial neurotoxins tetanus neurotoxin and botulinum neurotoxins (BoNTs), which cause tetanus and botulism, respectively. Specifically, SNAP-25 is cleaved by both BoNT/A and E at separate sites within the COOH-terminus. We now demonstrate, using toxin-insensitive mutants of SNAP-25, that these two toxins differ in their specificity for the cleavage site. Following modification within the COOH-terminus, the mutants completely resistant to BoNT/E do not bind VAMP but were still able to form a sodium dodecyl sulfate-resistant complex with VAMP and syntaxin. Furthermore, these mutants retain function in vivo, conferring BoNT/E-resistant exocytosis to transfected PC12 cells. These data provide information on structural requirements within the C-terminaldomain of SNAP-25 for its function in exocytosis and mise doubts about thesignificance of in vitro binary interactions for the in vivo functions of synaptic protein complexes.

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Documento generato il 07/07/20 alle ore 04:24:10