Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles.

Détails

ID Serval
serval:BIB_D3501FF53E4E
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles.
Périodique
Cell
Auteur⸱e⸱s
Mayer A., Wickner W., Haas A.
ISSN
0092-8674 (Print)
ISSN-L
0092-8674
Statut éditorial
Publié
Date de publication
1996
Volume
85
Numéro
1
Pages
83-94
Langue
anglais
Résumé
S. cerevisiae inherits its vacuole by projecting vacuole-derived membrane vesicles and tubules into the bud, where they fuse to establish the daughter vacuole. This homotypic fusion event can be assayed in vitro. It requires Sec17p and Sec18p, the homologs of the mammalian alpha-SNAP and NSF, which cooperate in multiple steps of membrane trafficking. We now report that Sec17p, Sec18p, and ATP are only needed for an early stage of the reaction that results in Sec17p release. Sec17p and Sec18p actions precede, and are needed for, the step employing the Ras-like GTPase Ypt7p. Sec18p-driven release of Sec17p can even precede vacuole docking, as it can occur prior to mixing of vacuoles and is insensitive to vacuole concentration. Sec17p and Sec18p thus may function in a predocking stage of the reaction, rather than in bilayer fusion per se.
Mots-clé
Adenosine Triphosphatases, Carrier Proteins/metabolism, Fungal Proteins/metabolism, GTP-Binding Proteins/metabolism, Kinetics, Membrane Fusion/physiology, Membrane Proteins/metabolism, Protein Binding/physiology, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins, Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins, Time Factors, Vacuoles/chemistry, Vacuoles/metabolism, Vesicular Transport Proteins, rab GTP-Binding Proteins, ras Proteins/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:06
Dernière modification de la notice
20/08/2019 16:53
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