SNAP-25 can self-associate to form a disulfide-linked complex

Détails

ID Serval
serval:BIB_12455815DBC4
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
SNAP-25 can self-associate to form a disulfide-linked complex
Périodique
Biological Chemistry
Auteur(s)
Sadoul  K., Berger  A., Niemann  H., Regazzi  R., Catsicas  S., Halban  P. A.
ISSN
1431-6730 (Print)
Statut éditorial
Publié
Date de publication
10/1997
Volume
378
Numéro
10
Pages
1171-6
Notes
In Vitro
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Oct
Résumé
SNAP-25 is expressed in neurons and endocrine cells and is essential for exocytosis of neurotransmitters and peptide hormones. It has been shown to be involved in several interactions with other proteins of the secretion machinery. Here we show that SNAP-25 can self-associate to form a disulfide-linked complex. Complex formation is facilitated in vitro (in concentrated extracts or by immunoprecipitation). SNAP-25 complexes, however, also form when intact cells are treated with a membrane-permeable crosslinker indicating that SNAP-25 molecules exist in close proximity in vivo and could form complexes spontaneously. We also show that monomeric SNAP-25 and disulfide-linked SNAP-25 complexes are palmitoylated and that both can be cleaved by botulinum neurotoxin E.
Mots-clé
Animals Botulinum Toxins/chemistry Brain Chemistry Cell Membrane Permeability Cross-Linking Reagents/chemistry Disulfides/*chemistry *Membrane Proteins Nerve Tissue Proteins/*chemistry Neurons/chemistry Precipitin Tests Rats Synaptosomal-Associated Protein 25
Pubmed
Web of science
Création de la notice
24/01/2008 14:30
Dernière modification de la notice
20/08/2019 12:40
Données d'usage