Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide.

Details

Serval ID
serval:BIB_50EA0EA749D3
Type
Article: article from journal or magazin.
Collection
Publications
Title
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide.
Journal
EMBO Journal
Author(s)
Burkhardt P., Hattendorf D.A., Weis W.I., Fasshauer D.
ISSN
1460-2075 (Electronic)
ISSN-L
0261-4189
Publication state
Published
Issued date
2008
Peer-reviewed
Oui
Volume
27
Number
7
Pages
923-933
Language
english
Abstract
Sec1/Munc18-like (SM) proteins functionally interact with SNARE proteins in vesicular fusion. Despite their high sequence conservation, structurally disparate binding modes for SM proteins with syntaxins have been observed. Several SM proteins appear to bind only to a short peptide present at the N terminus of syntaxin, designated the N-peptide, while Munc18a binds to a 'closed' conformation formed by the remaining portion of syntaxin 1a. Here, we show that the syntaxin 16 N-peptide binds to the SM protein Vps45, but the remainder of syntaxin 16 strongly enhances the affinity of the interaction. Likewise, the N-peptide of syntaxin 1a serves as a second binding site in the Munc18a/syntaxin 1a complex. When the syntaxin 1a N-peptide is bound to Munc18a, SNARE complex formation is blocked. Removal of the N-peptide enables binding of syntaxin 1a to its partner SNARE SNAP-25, while still bound to Munc18a. This suggests that Munc18a controls the accessibility of syntaxin 1a to its partners, a role that might be common to all SM proteins.
Keywords
Animals, Binding Sites, Calorimetry, Crystallography, X-Ray, Membrane Proteins/metabolism, Models, Molecular, Munc18 Proteins/metabolism, Mutant Proteins/metabolism, Peptides/metabolism, Protein Binding, Protein Structure, Secondary, Rats, SNARE Proteins/metabolism, Syntaxin 1/chemistry, Syntaxin 1/metabolism, Thermodynamics, Vesicular Transport Proteins/metabolism
Pubmed
Web of science
Open Access
Yes
Create date
15/09/2011 8:07
Last modification date
20/08/2019 14:06
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