Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10748442 | Biochemical and Biophysical Research Communications | 2016 | 6 Pages |
Abstract
Pyruvate kinase M2 (PKM2) is a key enzyme of glycolysis which is highly expressed in many tumor cells, and plays an important role in the Warburg effect. In previous study, we found PIM2 phosphorylates PKM2 at Thr454 residue (Yu, etl 2013). However, the functions of PKM2 Thr454 modification in cancer cells still remain unclear. Here we find PKM2 translocates into the nucleus after Thr454 phosphorylation. Replacement of wild type PKM2 with a mutant (T454A) enhances mitochondrial respiration, decreases pentose phosphate pathway, and enhances chemosensitivity in A549Â cells. In addition, the mutant (T454A) PKM2 reduces xenograft tumor growth in nude mice. These findings demonstrate that PKM2 T454 phosphorylation is a potential therapeutic target in lung cancer.
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Authors
Zhenhai Yu, Liangqian Huang, Pengyun Qiao, Aifang Jiang, Li Wang, Tingting Yang, Shengjian Tang, Wei Zhang, Chune Ren,