Membrane scission driven by the PROPPIN Atg18.

Détails

ID Serval
serval:BIB_AB8FBF52B8AE
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Membrane scission driven by the PROPPIN Atg18.
Périodique
The EMBO Journal
Auteur(s)
Gopaldass N., Fauvet B., Lashuel H., Roux A., Mayer A.
ISSN
1460-2075 (Electronic)
ISSN-L
0261-4189
Statut éditorial
Publié
Date de publication
2017
Peer-reviewed
Oui
Volume
36
Numéro
22
Pages
3274-3291
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Résumé
Sorting, transport, and autophagic degradation of proteins in endosomes and lysosomes, as well as the division of these organelles, depend on scission of membrane-bound tubulo-vesicular carriers. How scission occurs is poorly understood, but family proteins bind these membranes. Here, we show that the yeast PROPPIN Atg18 carries membrane scission activity. Purified Atg18 drives tubulation and scission of giant unilamellar vesicles. Upon membrane contact, Atg18 folds its unstructured CD loop into an amphipathic α-helix that inserts into the bilayer. This allows the protein to engage its two lipid binding sites for PI3P and PI(3,5)P2 PI(3,5)P2 induces Atg18 oligomerization, which should concentrate lipid-inserted α-helices in the outer membrane leaflet and drive membrane tubulation and scission. The scission activity of Atg18 is compatible with its known roles in endo-lysosomal protein trafficking, autophagosome biogenesis, and vacuole fission. Key features required for membrane tubulation and scission by Atg18 are shared by other PROPPINs, suggesting that membrane scission may be a generic function of this protein family.

Mots-clé
Amino Acid Sequence, Autophagy, Autophagy-Related Proteins/chemistry, Autophagy-Related Proteins/metabolism, Cell Membrane/metabolism, Green Fluorescent Proteins/metabolism, Lipids/chemistry, Membrane Proteins/chemistry, Membrane Proteins/metabolism, Mutation/genetics, Peptides/chemistry, Phosphatidylinositol Phosphates/metabolism, Protein Multimerization, Protein Structure, Secondary, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/chemistry, Saccharomyces cerevisiae Proteins/metabolism, Sodium Chloride/pharmacology, Time-Lapse Imaging, Unilamellar Liposomes/metabolism, Vacuoles/metabolism, autophagy, endosomes, lysosomes, membrane fission, membrane traffic
Pubmed
Web of science
Open Access
Oui
Création de la notice
30/11/2017 21:38
Dernière modification de la notice
20/08/2019 15:15
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