A look beyond the QR code of SNARE proteins.

Détails

ID Serval
serval:BIB_1BE4B72B9C35
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
A look beyond the QR code of SNARE proteins.
Périodique
Protein science
Auteur⸱e⸱s
Yadav D., Hacisuleyman A., Dergai M., Khalifeh D., Abriata L.A., Peraro M.D., Fasshauer D.
ISSN
1469-896X (Electronic)
ISSN-L
0961-8368
Statut éditorial
Publié
Date de publication
09/2024
Peer-reviewed
Oui
Volume
33
Numéro
9
Pages
e5158
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Résumé
Soluble N-ethylmaleimide-sensitive factor Attachment protein REceptor (SNARE) proteins catalyze the fusion process of vesicles with target membranes in eukaryotic cells. To do this, they assemble in a zipper-like fashion into stable complexes between the membranes. Structural studies have shown that the complexes consist of four different helices, which we subdivide into Qa-, Qb-, Qc-, and R-helix on the basis of their sequence signatures. Using a combination of biochemistry, modeling and molecular dynamics, we investigated how the four different types are arranged in a complex. We found that there is a matching pattern in the core of the complex that dictates the position of the four fundamental SNARE types in the bundle, resulting in a QabcR complex. In the cell, several different cognate QabcR-SNARE complexes catalyze the different transport steps between the compartments of the endomembrane system. Each of these cognate QabcR complexes is compiled from a repertoire of about 20 SNARE subtypes. Our studies show that exchange within the four types is largely tolerated structurally, although some non-cognate exchanges lead to structural imbalances. This suggests that SNARE complexes have evolved for a catalytic mechanism, a mechanism that leaves little scope for selectivity beyond the QabcR rule.
Mots-clé
SNARE Proteins/chemistry, SNARE Proteins/metabolism, Humans, Models, Molecular, Molecular Dynamics Simulation, Animals, coiled coil, compartments, eukaryotic cell, four‐helix bundle, membrane fusion, snare protein, vesicle trafficking
Pubmed
Open Access
Oui
Création de la notice
30/08/2024 15:38
Dernière modification de la notice
05/09/2024 9:01
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