Membrane scission driven by the PROPPIN Atg18

Article Article scientifique Article Membrane scission driven by the PROPPIN Atg18 eng 2017 author Gopaldass Navin Andréw 634451 author Fauvet Bruno author Lashuel Hilal author Roux Aurélien 0000-0002-6088-0711 716946 author Mayer Andreas 762175 3274-3291 10.15252/embj.201796859 0261-4189 https://onlinelibrary.wiley.com/doi/abs/10.15252/embj.201796859 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. Dewey 540 39 Département de biochimie 144 false EMBO Journal 36 22 34a237b6-97ed-4859-9dbf-7f98f45bfb82 Article (Published version) Restricted Membrane_AR_17.pdf 10476758 application/pdf restrictedAccess Faculté des sciences / Section de chimie et biochimie / Département de biochimie

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Membrane scission driven by the PROPPIN Atg18	EMBO Journal			2017	280	0

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Mayer, Andreas