The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex.

Détails

Ressource 1Télécharger: Demircioglu-PNAS2014.pdf (4355.42 [Ko])
Etat: Public
Version: Final published version
ID Serval
serval:BIB_64C8A3798C53
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex.
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur⸱e⸱s
Demircioglu F.E., Burkhardt P., Fasshauer D.
ISSN
1091-6490 (Electronic)
ISSN-L
0027-8424
Statut éditorial
Publié
Date de publication
2014
Peer-reviewed
Oui
Volume
111
Numéro
38
Pages
13828-13833
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't Publication Status: ppublish
Résumé
Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins constitute the core of an ancient vesicle fusion machine that diversified into distinct sets that now function in different trafficking steps in eukaryotic cells. Deciphering their precise mode of action has proved challenging. SM proteins are thought to act primarily through one type of SNARE protein, the syntaxins. Despite high structural similarity, however, contrasting binding modes have been found for different SM proteins and syntaxins. Whereas the secretory SM protein Munc18 binds to the ‟closed conformation" of syntaxin 1, the ER-Golgi SM protein Sly1 interacts only with the N-peptide of Sed5. Recent findings, however, indicate that SM proteins might interact simultaneously with both syntaxin regions. In search for a common mechanism, we now reinvestigated the Sly1/Sed5 interaction. We found that individual Sed5 adopts a tight closed conformation. Sly1 binds to both the closed conformation and the N-peptide of Sed5, suggesting that this is the original binding mode of SM proteins and syntaxins. In contrast to Munc18, however, Sly1 facilitates SNARE complex formation by loosening the closed conformation of Sed5.
Pubmed
Web of science
Open Access
Oui
Création de la notice
07/09/2014 15:41
Dernière modification de la notice
20/08/2019 15:21
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