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- W4205855953 abstract "Abstract Dimer-tetramer transition determines the pyruvate kinase activity of pyruvate kinase M2 (PKM2), the final rate-limiting enzyme in glycolysis. Several small molecules have been shown to be able to promote PKM2 confirmation change, but the role of oncoproteins including the cancerous inhibitor of protein phosphatase PP2A (CIP2A) that is overexpressed in most human malignancies, in PKM2 dimer-tetramer transition remains largely unknown. Here we reported that CIP2A inhibited glycolysis and promoted oxidative metabolism in non-small cell lung cancer (NSCLC) cells. CIP2A directly bound PKM2 and induced formation of PKM2 tetramer, whereas CIP2A depletion resulted in reduced tetrameric and increased dimeric forms of PKM2. We found that serine 287 of PKM2 was essential for PKM2 dimer-tetramer switching, whereas mutation in this residue abrogated CIP2A-induced tetramer formation and pyruvate kinase activity increment. Clinically, the expression of CIP2A was positively associated with the level of phosphorylated PKM2 S287, and CIP2A high / PKM2 high and PKM2 high / CIP2A high were associated with poor prognosis of NSCLC patients. Pharmacological inhibition of glycolysis or activation of PKM2 synergistically inhibited NSCLC cell growth when combined with CIP2A-targeting compound celastrol both in vitro and in vivo . These results demonstrated that CIP2A determines PKM2 dimer-tetramer transition and controls the metabolic reprogramming of NSCLC cells." @default.
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- W4205855953 date "2022-01-19" @default.
- W4205855953 modified "2023-10-04" @default.
- W4205855953 title "Oncoprotein CIP2A controls PKM2 dimer-tetramer transition through phosphorylation of serine 287 in non-small cell lung cancer" @default.
- W4205855953 doi "https://doi.org/10.21203/rs.3.rs-1232624/v1" @default.
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