ArticleCell death and differentiation2026
Histone deacetylase 6 deacetylates and ubiquitinates ATG3 to regulate autophagy.
Article in Cell death and differentiation, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Quinazolinone and Phthalazinone Inhibitors of the HDAC6/Ubiquitin Protein-Protein Interaction.Chembiochem : a European journal of chemical biology · 2026Article
- Quinazolinone and Phthalazinone Inhibitors of the HDAC6/Ubiquitin Protein-Protein Interaction.bioRxiv : the preprint server for biology · 2025Article
- Crosstalk Between Allergic Inflammation and Autophagy.International journal of molecular sciences · 2025Review
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Authors and funding
7 authors.
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Abstract
ATG3 (autophagy-related gene 3), an E2 like enzyme, plays a vital role in autophagy by regulating the lipidation modification of LC3 (microtubule-associated protein 1A/1B-light chain 3). Although the level of ATG3 can be reduced by the ubiquitin-proteasome pathway, the detailed mechanisms of this regulation remain elusive. Histone deacetylase 6 (HDAC6) is involved in multiple cellular activities by regulating acetylation of its substrates such as α-tubulin and cortactin. Here, we revealed a novel function of HDAC6 in autophagy regulation by mediating the post-translational modifications of ATG3. We found that HDAC6 interacts with ATG3 and deacetylates ATG3. In addition, HDAC6 acts its ubiquitin E3 ligase activity and ubiquitinates ATG3 at lysine 272, leading to ATG3 degradation. Intriguingly, lysine 272 of ATG3 is targeted for deacetylation as well as ubiquitination by HDAC6. Further study showed that HDAC6 participates in autophagy by mediating ATG3 degradation. Taken together, our findings uncover a novel role of HDAC6 in autophagy regulation by mediating the protein modification and degradation of ATG3.
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