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research article

Membrane scission driven by the PROPPIN Atg18

Gopaldass, Navin
•
Fauvet, Bruno  
•
Lashuel, Hilal  
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2017
Embo Journal

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 a-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 a-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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Type
research article
DOI
10.15252/embj.201796859
Web of Science ID

WOS:000415184300003

Author(s)
Gopaldass, Navin
Fauvet, Bruno  
Lashuel, Hilal  
Roux, Aurélien
Mayer, Andreas
Date Issued

2017

Publisher

Nature Publishing Group

Published in
Embo Journal
Volume

36

Issue

22

Start page

3274

End page

3291

Subjects

autophagy

•

endosomes

•

lysosomes

•

membrane fission

•

membrane traffic

URL

URL

http://emboj.embopress.org/content/early/2017/10/13/embj.201796859
Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LMNN  
Available on Infoscience
September 11, 2017
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/140627
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