<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>12</volume><submitter>Ohba S</submitter><pubmed_abstract>PKM2 is a phosphotyrosine-binding glycolytic enzyme upregulated in many cancers, including glioma, and contributes to tumor growth by regulating cell cycle progression. We noted, however, that in multiple glioma cell lines, PKM2 knock-down resulted in an accumulation of cells in G2-M phase. Moreover, PKM2 knock-down decreased Cdk1 activity while introducing a constitutively active Cdk1 reversed the effects of PKM2 knock-down on cell cycle progression. The means by which PKM2 increases Cdk1 activity have not been described. Transient interaction of T14/Y15-phosphorylated Cdk1 with cyclin B allows Cdk7-mediated pT161 Cdk1 phosphorylation followed by cdc25C-mediated removal of pT14/Y15 and activation of Cdk1 in cycling cells. In the present course of investigation, PKM2 modulation did not inf</pubmed_abstract><journal>Frontiers in oncology</journal><pagination>844861</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8981990</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>PKM2 Interacts With the Cdk1-CyclinB Complex to Facilitate Cell Cycle Progression in Gliomas.</pubmed_title><pmcid>PMC8981990</pmcid><pubmed_authors>Mukherjee J</pubmed_authors><pubmed_authors>Johannessen TA</pubmed_authors><pubmed_authors>Ohba S</pubmed_authors><pubmed_authors>Tang Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>PKM2 Interacts With the Cdk1-CyclinB Complex to Facilitate Cell Cycle Progression in Gliomas.</name><description>PKM2 is a phosphotyrosine-binding glycolytic enzyme upregulated in many cancers, including glioma, and contributes to tumor growth by regulating cell cycle progression. We noted, however, that in multiple glioma cell lines, PKM2 knock-down resulted in an accumulation of cells in G2-M phase. Moreover, PKM2 knock-down decreased Cdk1 activity while introducing a constitutively active Cdk1 reversed the effects of PKM2 knock-down on cell cycle progression. The means by which PKM2 increases Cdk1 activity have not been described. Transient interaction of T14/Y15-phosphorylated Cdk1 with cyclin B allows Cdk7-mediated pT161 Cdk1 phosphorylation followed by cdc25C-mediated removal of pT14/Y15 and activation of Cdk1 in cycling cells. In the present course of investigation, PKM2 modulation did not inf</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2025-05-18T12:05:53.659Z</modification><creation>2025-05-18T12:05:53.659Z</creation></dates><accession>S-EPMC8981990</accession><cross_references><pubmed>35392228</pubmed><doi>10.3389/fonc.2022.844861</doi></cross_references></HashMap>