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Related Experiment Videos

Membrane scission driven by the PROPPIN Atg18.

Navin Gopaldass1, Bruno Fauvet2, Hilal Lashuel2

  • 1Department of Biochemistry, University of Lausanne, Epalinges, Switzerland.

The EMBO Journal
|October 15, 2017
PubMed
Summary
This summary is machine-generated.

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The yeast protein Atg18 performs membrane scission, a crucial step in organelle division and protein trafficking. This PROPPIN protein

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Membrane scission of tubulo-vesicular carriers is essential for endosome-lysosome function and organelle division.
  • The precise mechanism of membrane scission remains poorly understood.
  • PROPPIN proteins are known to interact with cellular membranes.

Purpose of the Study:

  • To investigate the membrane scission activity of the yeast PROPPIN protein, Atg18.
  • To elucidate the molecular mechanism by which Atg18 mediates membrane scission.
  • To determine if membrane scission is a conserved function of the PROPPIN family.

Main Methods:

  • Purification of yeast Atg18 protein.
  • In vitro assays using giant unilamellar vesicles (GUVs) to assess tubulation and scission.
Keywords:
autophagyendosomeslysosomesmembrane fissionmembrane traffic

Related Experiment Videos

  • Lipid-binding assays to identify phosphoinositide interactions.
  • Structural analysis of Atg18 upon membrane interaction.

    • Main Results:

    • Purified Atg18 protein exhibits membrane tubulation and scission activity on GUVs.
    • Atg18 inserts an amphipathic α-helix into the lipid bilayer upon membrane contact.
    • Atg18 binds phosphatidylinositol 3-phosphate (PI3P) and phosphatidylinositol (3,5)-bisphosphate (PI(3,5)P2).
    • PI(3,5)P2 binding induces Atg18 oligomerization, concentrating lipid-inserted helices and driving scission.

    Conclusions:

    • Yeast Atg18 possesses intrinsic membrane scission activity, crucial for endo-lysosomal trafficking and organelle division.
    • The mechanism involves lipid-induced conformational changes and oligomerization, leading to membrane deformation and scission.
    • Shared functional features suggest membrane scission may be a general capability of the PROPPIN protein family.