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Membrane scission driven by the PROPPIN Atg18.

  • Gopaldass N Department of Biochemistry, University of Lausanne, Epalinges, Switzerland.
  • Fauvet B Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
  • Lashuel H Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
  • Roux A Department of Biochemistry, University of Geneva, Geneva, Switzerland.
  • Mayer A Department of Biochemistry, University of Lausanne, Epalinges, Switzerland andreas.mayer@unil.ch.
  • 2017-10-15
Published in:
  • The EMBO journal. - 2017
autophagy
endosomes
lysosomes
membrane fission
membrane traffic
Amino Acid Sequence
Autophagy
Autophagy-Related Proteins
Cell Membrane
Green Fluorescent Proteins
Lipids
Membrane Proteins
Mutation
Peptides
Phosphatidylinositol Phosphates
Protein Multimerization
Protein Structure, Secondary
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sodium Chloride
Time-Lapse Imaging
Unilamellar Liposomes
Vacuoles
English 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.
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  • English
Open access status
green
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Persistent URL
https://sonar.ch/global/documents/149449
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