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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
Summary
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.
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.
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