4.7 Article

Deubiquitination of MYC by OTUB1 contributes to HK2 mediated glycolysis and breast tumorigenesis

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CELL DEATH AND DIFFERENTIATION
卷 29, 期 9, 页码 1864-1873

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SPRINGERNATURE
DOI: 10.1038/s41418-022-00971-8

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资金

  1. National Natural Science Foundation of China [81972489, 82003201]
  2. National Natural Science Foundation of Shandong Province [ZR2020YQ58, ZR2020QH255]
  3. Taishan Scholar Program of Shandong Province [tsqn202103113]
  4. Shandong Province College Science and Technology Plan Project [J17KA254]
  5. Projects of medical and health technology development program in Shandong province [2018WS057]

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OTUB1 is identified as a new deubiquitination enzyme for MYC protein degradation, promoting breast tumorigenesis by stabilizing MYC and enhancing its transcriptional activity and aerobic glycolysis.
MYC as a transcriptional factor plays a crucial role in breast cancer progression. However, the mechanisms underlying MYC deubiquitination in breast cancer are not well defined. Here, we report that OTUB1 is responsible for MYC deubiquitination. OTUB1 could directly deubiquitinate MYC at K323 site, which blocks MYC protein degradation. Moreover, OTUB1 mediated MYC protein stability is also confirmed in OTUB1-knockout mice. Stabilized MYC by OTUB1 promotes its transcriptional activity and induces HK2 expression, which leads to enhance aerobic glycolysis. Therefore, OTUB1 promotes breast tumorigenesis in vivo and in vitro via blocking MYC protein degradation. Taken together, our data identify OTUB1 as a new deubiquitination enzyme for MYC protein degradation, which provides a potential target for breast cancer treatment.

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