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LC3 conjugation to lipid droplets.

Mohyeddine Omrane1, Thomas J Melia2, Abdou Rachid Thiam1

  • 1Laboratoire de Physique de L'École Normale Supérieure, ENS, Université PSL, CNRS, Sorbonne Université, Université Paris Cité, Paris, France.

Autophagy
|August 21, 2023
PubMed
Summary

Macroautophagy/autophagy involves lipid droplet (LD) degradation. Our study reveals a non-canonical role for LDs in autophagy, where ATG3 on LDs facilitates LC3B lipidation and phagophore tethering for degradation.

Keywords:
ATG3LC3Blipid dropletsmembrane contact sitesnoncanonical autophagyprolonged starvation

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Macroautophagy/autophagy and lipid droplet (LD) biology are closely interconnected.
  • LDs are implicated in autophagosome formation, potentially supplying lipids and acting as assembly platforms.
  • Shared proteins between LDs and autophagosomes suggest overlapping functions, but these remain unclear.

Purpose of the Study:

  • To investigate the non-canonical role of lipid droplets (LDs) in autophagy.
  • To elucidate the function of ATG3 and LC3B in the context of LDs during starvation.

Main Methods:

  • Cell starvation experiments to observe protein localization.
  • In vitro assays using purified and artificial LDs.
  • Microscopy to analyze LD-LC3B interactions and autophagosome formation.

Main Results:

  • Prolonged starvation induced ATG3 localization to large LDs, promoting LC3B lipidation.
  • ATG3 was found to associate with LDs in vitro, binding conjugated Atg8-family proteins.
  • LC3B on LDs acted as a tether, connecting phagophores to LDs for lysosome-mediated degradation.

Conclusions:

  • Lipid droplets (LDs) possess a previously unrecognized non-canonical role in autophagy.
  • LD-associated LC3B may serve as a crucial tethering factor, linking autophagosomes to LDs for degradation.
  • Certain LD surfaces might function as lipidation sites for LC3B, facilitating autophagosome biogenesis.