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Deubiquitination of ME1 by OTUD7B promotes aerobic glycolysis of esophageal cancer
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DOI：10.1016/j.bcp.2026.118340.png)
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Abstract
En 中文
Esophageal cancer (EC) is among the most prevalent malignancies worldwide. Malic enzyme 1 (ME1), which catalyzes the oxidative decarboxylation of malate to pyruvate, contributes to the Warburg effect (aerobic glycolysis) and plays a pivotal role in the progression of tumor growth. Nevertheless, the functional contribution of ME1 to EC growth via aerobic glycolysis remains unclear. This study aimed to investigate the role of ME1 in EC and the underlying mechanisms. In this study, we discovered a close association between ME1 expression and poor patient outcomes. Altered ME1 expression increased or decreased EC aerobic glycolysis and progression. Mechanistically, the deubiquitinating enzyme (DUB) OTU Deubiquitinase 7B (OTUD7B) deubiquitinated and stabilized ME1. Furthermore, ME1 overexpression reversed the effects of OTUD7B knockdown on aerobic glycolysis and tumor growth in vivo. These findings suggested that OTUD7B functions as a key DUB that regulates ME1 at the posttranslational level, and these results offer a promising strategy for treating EC metastasis. Knockdown of OTUD7B or ME1 inhibited cell proliferation, colony formation, and tumorigenesis. In addition, ME1 overexpression in OTUD7B-deficient EC cells restored cell viability. These results suggested that deubiquitination regulates ME1 function by stabilizing it in vivo. Our findings demonstrated that ME1 promotes the Warburg effect and is stabilized by OTUD7B. These results highlight the potential of targeting ME1 and OTUD7B in the treatment of human EC.
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