ArticleFrontiers in oncology2026
The deubiquitinating enzyme UCHL3 promotes bladder cancer progression and glycolysis through enhancing PKM2 protein stability.
Article in Frontiers in oncology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Pyruvate kinase M2 (PKM2) is a critical rate-limiting enzyme in glycolysis and is frequently upregulated in bladder cancer (BCa), contributing to the Warburg effect and tumor progression. However, the mechanism supporting abnormal PKM2 stabilization via deubiquitination in BCa remains to be characterized. Here, we identified ubiquitin C-terminal hydrolase L3 (UCHL3) as a bona fide deubiquitylase of PKM2 in BCa. UCHL3 stabilized PKM2 in a deubiquitylation activity-dependent manner. UCHL3 depletion significantly decreased PKM2 protein levels, suppressed glycolytic activity, and inhibited BCa cell proliferation, colony formation, migration
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