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The ULK1 effector BAG2 regulates autophagy initiation by modulating AMBRA1 localization.

Devanarayanan Siva Sankar1, Stephanie Kaeser-Pebernard1, Christine Vionnet1

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|August 29, 2024
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Autophagy initiation involves the ULK1 complex interacting with kinases and autophagy receptors. ULK1 phosphorylates BAG2 under starvation, promoting autophagy by regulating AMBRA1 localization.

Keywords:
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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Autophagy is a fundamental cellular process for degrading damaged components.
  • The ULK1 complex is a key initiator of autophagy.
  • Understanding the ULK1 complex's regulation and interactions is crucial for deciphering autophagy pathways.

Purpose of the Study:

  • To comprehensively map the ULK1 complex interactome.
  • To investigate the role of ULK1 complex interactions in response to nutrient starvation.
  • To elucidate the regulatory mechanism of autophagy initiation involving BAG2 and AMBRA1.

Main Methods:

  • Affinity purification-mass spectrometry
  • Proximity labeling-mass spectrometry
  • Analysis of protein-protein interactions
  • Phosphorylation site mapping

Main Results:

  • A deep interactome of the ULK1 complex (ULK1, ATG13, ATG101, RB1CC1/FIP200) was generated.
  • The ULK1 complex interacts with kinases, phosphatases, and selective autophagy receptors under starvation.
  • ULK1-mediated phosphorylation of BAG2 on Ser31 under starvation promotes AMBRA1 recruitment to the ER, enhancing autophagy.

Conclusions:

  • The ULK1 complex forms a signalosome that integrates starvation signals.
  • Nutrient starvation activates selective autophagy pathways via ULK1 complex interactions.
  • BAG2 acts as a nutritional sensor, with its phosphorylation state by ULK1 dynamically regulating autophagy induction.