Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion.

Détails

ID Serval
serval:BIB_F9D156A2A5E0
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion.
Périodique
Nature
Auteur(s)
Peters C., Bayer M.J., Bühler S., Andersen J.S., Mann M., Mayer A.
ISSN
0028-0836 (Print)
ISSN-L
0028-0836
Statut éditorial
Publié
Date de publication
2001
Volume
409
Numéro
6820
Pages
581-588
Langue
anglais
Résumé
SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) and Rab-GTPases, together with their cofactors, mediate the attachment step in the membrane fusion of vesicles. But how bilayer mixing--the subsequent core process of fusion--is catalysed remains unclear. Ca2+/calmodulin controls this terminal process in many intracellular fusion events. Here we identify V0, the membrane-integral sector of the vacuolar H+-ATPase, as a target of calmodulin on yeast vacuoles. Between docking and bilayer fusion, V0 sectors from opposing membranes form complexes. V0 trans-complex formation occurs downstream from trans-SNARE pairing, and depends on both the Rab-GTPase Ypt7 and calmodulin. The maintenance of existing complexes and completion of fusion are independent of trans-SNARE pairs. Reconstituted proteolipids form sealed channels, which can expand to form aqueous pores in a Ca2+/calmodulin-dependent fashion. V0 trans-complexes may therefore form a continuous, proteolipid-lined channel at the fusion site. We propose that radial expansion of such a protein pore may be a mechanism for intracellular membrane fusion.
Mots-clé
Calmodulin/metabolism, Cell Membrane, Membrane Fusion, Membrane Proteins/metabolism, Protein Binding, Proteolipids/metabolism, Proton Pumps/metabolism, Proton-Translocating ATPases/metabolism, SNARE Proteins, Vesicular Transport Proteins, Yeasts
Pubmed
Web of science
Création de la notice
24/01/2008 16:06
Dernière modification de la notice
03/03/2018 22:54
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