Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion‐to‐fusion transition

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ID Serval
serval:BIB_63B85777BBAC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion‐to‐fusion transition
Périodique
EMBO Reports
Auteur(s)
D'Agostino Massimo, Risselada Herre Jelger, Mayer Andreas
ISSN
1469-3178
ISSN-L
1469-221X
Statut éditorial
Publié
Date de publication
2016
Peer-reviewed
Oui
Volume
17
Numéro
11
Pages
1590-1608
Langue
anglais
Résumé
SNAREs fuse membranes in several steps. Trans-SNARE complexes juxtapose membranes, induce hemifused stalk structures, and open the fusion pore. A recent penetration model of fusion proposed that SNAREs force the hydrophilic C-termini of their transmembrane domains through the hydrophobic core of the membrane(s). In contrast, the indentation model suggests that the C-termini open the pore by locally compressing and deforming the stalk. Here we test these models in the context of yeast vacuole fusion. Addition of small hydrophilic tags renders bilayer penetration by the C-termini energetically unlikely. It preserves fusion activity, however, arguing against the penetration model. Addition of large protein tags to the C-termini permits SNARE activation, trans-SNARE pairing, and hemifusion but abolishes pore opening. Fusion proceeds if the tags are detached from the membrane by a hydrophilic spacer or if only one side of the trans-SNARE complex carries a protein tag. Thus, both sides of a trans-SNARE complex can drive pore opening. Our results are consistent with an indentation model in which multiple SNARE C-termini cooperate in opening the fusion pore by locally deforming the inner leaflets.
Mots-clé
exocytosis, lysosome, membrane fusion, SNAREs, vacuole
Pubmed
Web of science
Open Access
Oui
Création de la notice
01/12/2016 8:17
Dernière modification de la notice
20/08/2019 14:20
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