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Related Experiment Video

Updated: Aug 24, 2025

Exploring the Regulation of Lipid Droplet Catabolism through Lipophagy
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Acyl-CoA binding protein regulates nutrient-dependent autophagy.

Prajna Udupa1, Abhishek Kumar2, Rahul Parit1

  • 1Departmentof Medical Genetics, Kasturba Medical College, Manipal Academy of Higher Education, Manipal, Karnataka 576104, India.

Metabolism: Clinical and Experimental
|October 24, 2022
PubMed
Summary

Diazepam-binding inhibitor (DBI) suppresses autophagy by binding to phagophore membranes. Nutrient starvation triggers DBI phosphorylation, releasing it to activate autophagy initiation and phagophore maturation.

Keywords:
AutophagyDiazepam-binding inhibitorNutrient stressPhosphorylationProtein-lipid binding

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Autophagy homeostasis relies on regulatory proteins, but the protein-lipid interactions controlling autophagy initiation remain unclear.
  • Understanding the switch between autophagy suppression and activation is crucial for cellular regulation.

Purpose of the Study:

  • To elucidate the role of protein-lipid interactions in regulating autophagy initiation.
  • To identify the molecular mechanisms by which diazepam-binding inhibitor (DBI) controls autophagy.

Main Methods:

  • Investigated the interaction between human diazepam-binding inhibitor (DBI) and phosphatidylethanolamine on phagophore membranes.
  • Utilized techniques to analyze the effect of DBI phosphorylation on its binding affinity and autophagy regulation.
  • Examined the impact of AMP-activated protein kinase (AMPK) on DBI phosphorylation and subsequent autophagy flux.

Main Results:

  • Human diazepam-binding inhibitor (DBI), also known as acyl-CoA binding protein (ACBP), binds to phosphatidylethanolamine (PE) on phagophore membranes under nutrient-rich conditions, inhibiting LC3 lipidation and autophagy.
  • Specific tyrosine residues in DBI are critical for stabilizing PE within its acyl-CoA binding cavity.
  • AMP-activated protein kinase (AMPK)-mediated phosphorylation of DBI at serine-21 under starvation drastically reduces its affinity for PE, promoting autophagy initiation.

Conclusions:

  • DBI acts as a critical regulator, preventing excessive autophagy under nutrient-rich conditions and promoting it during nutrient deficiency.
  • Phosphorylation of DBI by AMPK is a key event that switches autophagy from a suppressed to an activated state.
  • The dynamic interaction of DBI with phagophore membranes, modulated by phosphorylation, is essential for controlling autophagosome formation.