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Related Experiment Video

Updated: Jan 30, 2026

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
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Acetylation modulates LC3 stability and cargo recognition.

Tingting Song1, Haifeng Su2, Wei Yin3

  • 1Life Sciences Institute, Zhejiang University, Hangzhou, China.

FEBS Letters
|January 12, 2019
PubMed
Summary
This summary is machine-generated.

Acetylation stabilizes microtubule-associated protein 1A/1B-light chain 3 (LC3), a key autophagy protein. This acetylation prevents cargo receptor p62 mis-targeting, ensuring efficient cellular waste degradation.

Keywords:
LC3acetylationautophagyp62

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Microtubule-associated protein 1A/1B-light chain 3 (LC3) is crucial for autophagy, mediating autophagosome formation and cargo recruitment.
  • While deacetylated LC3 performs these functions, the acetylated form is more abundant, suggesting a regulatory role for acetylation.

Purpose of the Study:

  • To investigate the impact of LC3 acetylation on its stability and cargo recognition.
  • To elucidate the mechanism by which acetylation influences LC3 interactions and autophagic degradation.

Main Methods:

  • Fluorescence recovery after photobleaching (FRAP) was used to measure the diffusion rate of soluble LC3.
  • Investigated the interaction between acetylated LC3 and the autophagic cargo receptor p62.

Main Results:

  • Nutrient-state-dependent acetylation inhibits LC3 complex formation and its interaction with p62.
  • Acetylation prevents p62 mis-targeting to non-autophagic LC3, facilitating efficient cargo degradation.
  • Acetylation also inhibits proteasome-dependent degradation of LC3, promoting its stability as a reserve protein.

Conclusions:

  • LC3 acetylation acts as a regulatory mechanism controlling its function and stability.
  • Acetylated LC3 serves as a stable, non-activated reserve, preventing premature or inappropriate interactions and ensuring efficient autophagic degradation when needed.