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Article

Regulation of pyruvate kinase isozyme M2 is mediated by the ubiquitin-specific protease 20

  • Authors:
    • So-Ra Kim
    • Jin-Ock Kim
    • Key-Hwan Lim
    • Ji-Hyun Yun
    • Inbo Han
    • Kwang-Hyun Baek
  • View Affiliations / Copyright

    Affiliations: Department of Biomedical Science, CHA University, Bundang CHA General Hospital, Gyeonggi-Do 463-400, Republic of Korea, Department of Neurosurgery, CHA University, Bundang CHA General Hospital, Gyeonggi-Do 463-400, Republic of Korea
  • Pages: 2116-2124
    |
    Published online on: February 19, 2015
       https://doi.org/10.3892/ijo.2015.2901
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Abstract

USP20, one of deubiquitinating enzymes (DUBs) belonging to the subfamily of ubiquitin-specific protease (USP), regulates ubiquitin-mediated protein degradation. So far, USP20 has been identified as a binding protein and a regulator of hypoxia-inducible factor (HIF)-1α, β-adrenergic receptor, and tumor necrosis factor (TNF) receptor associated factor 6 (TRAF6). In order to investigate other biological functions of USP20 with its novel substrates, we searched for putative substrates through two-dimensional electrophoresis (2-DE) and matrix-assisted laser desorption-ionization time-of-flight mass spectrometry (MALDI-TOF/MS) analysis. We found several putative substrates, some of which are related to cancer metabolism or neural disorders. Among these, the pyruvate kinase isoenzyme M2 (PKM2) had a high identity score. Most cancer cells contain a specific metabolic pathway, referred to as the Warburg effect. One well-known function of PKM2 is a main regulator in cancer metabolic pathways, and PKM2 promotes the Warburg effect and tumor growth. In addition, both PKM2 and HIF-1α upregulate the expression of target genes. From this evidence, it is expected that USP20 would be associated with the metabolic pathway through the regulation of PKM2 ubiquitination. Despite various roles of DUBs, the biological functions of USP20 in cellular mechanisms are poorly understood. Herein, we investigated the inter­action between PKM2 and USP20. Our results suggest a new molecular pathway in cancer metabolism through the regulation of PKM2.
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Copy and paste a formatted citation
Spandidos Publications style
Kim S, Kim J, Lim K, Yun J, Han I and Baek K: Regulation of pyruvate kinase isozyme M2 is mediated by the ubiquitin-specific protease 20. Int J Oncol 46: 2116-2124, 2015.
APA
Kim, S., Kim, J., Lim, K., Yun, J., Han, I., & Baek, K. (2015). Regulation of pyruvate kinase isozyme M2 is mediated by the ubiquitin-specific protease 20. International Journal of Oncology, 46, 2116-2124. https://doi.org/10.3892/ijo.2015.2901
MLA
Kim, S., Kim, J., Lim, K., Yun, J., Han, I., Baek, K."Regulation of pyruvate kinase isozyme M2 is mediated by the ubiquitin-specific protease 20". International Journal of Oncology 46.5 (2015): 2116-2124.
Chicago
Kim, S., Kim, J., Lim, K., Yun, J., Han, I., Baek, K."Regulation of pyruvate kinase isozyme M2 is mediated by the ubiquitin-specific protease 20". International Journal of Oncology 46, no. 5 (2015): 2116-2124. https://doi.org/10.3892/ijo.2015.2901
Copy and paste a formatted citation
x
Spandidos Publications style
Kim S, Kim J, Lim K, Yun J, Han I and Baek K: Regulation of pyruvate kinase isozyme M2 is mediated by the ubiquitin-specific protease 20. Int J Oncol 46: 2116-2124, 2015.
APA
Kim, S., Kim, J., Lim, K., Yun, J., Han, I., & Baek, K. (2015). Regulation of pyruvate kinase isozyme M2 is mediated by the ubiquitin-specific protease 20. International Journal of Oncology, 46, 2116-2124. https://doi.org/10.3892/ijo.2015.2901
MLA
Kim, S., Kim, J., Lim, K., Yun, J., Han, I., Baek, K."Regulation of pyruvate kinase isozyme M2 is mediated by the ubiquitin-specific protease 20". International Journal of Oncology 46.5 (2015): 2116-2124.
Chicago
Kim, S., Kim, J., Lim, K., Yun, J., Han, I., Baek, K."Regulation of pyruvate kinase isozyme M2 is mediated by the ubiquitin-specific protease 20". International Journal of Oncology 46, no. 5 (2015): 2116-2124. https://doi.org/10.3892/ijo.2015.2901
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