{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["16(1)"],"submitter":["Zhao J"],"pubmed_abstract":["Metabolic alterations in chondrocytes play a crucial role in the progression of temporomandibular joint osteoarthritis (TMJOA). However, the precise molecular mechanisms underlying these changes remain poorly understood. In this study, we identify ubiquitin-specific protease 32 (USP32) as a key regulator of TMJOA progression through its interaction with pyruvate kinase M2 (PKM2), a vital enzyme in glycolysis. Our results demonstrate that USP32 is significantly upregulated in TMJOA cartilage and inflammatory chondrocytes. USP32 stabilizes PKM2 by removing K48- and K11-linked ubiquitin chains, thereby preventing its proteasomal degradation. This stabilization promotes the accumulation of PKM2, leading to enhanced glycolysis, increased lactate production, and mitochondrial dysfunction, all of"],"journal":["Cell death & disease"],"pagination":["781"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12583448"],"repository":["biostudies-literature"],"pubmed_title":["USP32 promotes temporomandibular joint osteoarthritis by modulating PKM2 stability and glycolytic metabolism in chondrocytes."],"pmcid":["PMC12583448"],"pubmed_authors":["Wang M","Liu Z","Feng Z","Du T","Qi K","Li R","Zhao J","Li M"],"additional_accession":[]},"is_claimable":false,"name":"USP32 promotes temporomandibular joint osteoarthritis by modulating PKM2 stability and glycolytic metabolism in chondrocytes.","description":"Metabolic alterations in chondrocytes play a crucial role in the progression of temporomandibular joint osteoarthritis (TMJOA). However, the precise molecular mechanisms underlying these changes remain poorly understood. In this study, we identify ubiquitin-specific protease 32 (USP32) as a key regulator of TMJOA progression through its interaction with pyruvate kinase M2 (PKM2), a vital enzyme in glycolysis. Our results demonstrate that USP32 is significantly upregulated in TMJOA cartilage and inflammatory chondrocytes. USP32 stabilizes PKM2 by removing K48- and K11-linked ubiquitin chains, thereby preventing its proteasomal degradation. This stabilization promotes the accumulation of PKM2, leading to enhanced glycolysis, increased lactate production, and mitochondrial dysfunction, all of","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-05T11:49:03.299Z","creation":"2026-05-16T03:13:22.131Z"},"accession":"S-EPMC12583448","cross_references":{"pubmed":["41184228"],"doi":["10.1038/s41419-025-08053-6"]}}