ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026
Acetylation Regulates ACSL4 Degradation Through Chaperone-Mediated Autophagy to Alleviate Intervertebral Disc Degeneration.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- ACSL4-Dependent Lysosomal Lipid Peroxidation Links WTAP-Mediated mAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Lactylation and acetylation: parallel paths, divergent deeds, and research dilemmas.Journal of translational medicine · 2026Review
- Acetylation Regulates ACSL4 Degradation Through Chaperone-Mediated Autophagy to Alleviate Intervertebral Disc Degeneration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Protein Post-Translational Modifications in the Regulation of Ferroptosis: New Opportunities and Challenges for Cancer Immunotherapy.International journal of biological sciences · 2026Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Chaperone-mediated autophagy (CMA) represents a critical lysosomal degradation pathway in the context of intervertebral disc degeneration (IVDD) associated with senescence. This study revealed a novel mechanism of CMA regulation involving targeted degradation of acyl-CoA synthetase long-chain family member 4 (ACSL4), which can delay nucleus pulposus cell (NPC) senescence and inhibit IVDD progression. Mechanistic investigations demonstrated that the acetyltransferase KAT2B can facilitate the acetylation of ACSL4 at lysine residues K500, K571, and K692. This post-translational modification served as a molecular switch, significantly enhancing the affinity between ACSL4 and the CMA recognition chaperone HSPA8, thereby promoting the efficient targeting and degradation of ACSL4 via the CMA pathway. Besides, engineered exosomes are harnessed to deliver the key CMA receptor LAMP2A in an in vivo model, effectively delaying cellular senescence and significantly attenuating IVDD progression. Overall, these findings establish the crucial protective role of CMA in preventing IVDD through the degradation of ACSL4, providing novel insights for developing therapeutic strategies targeting CMA activation to alleviate disc degeneration and associated chronic pain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.