{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Peng J"],"funding":["U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences","University of Kentucky (UK)","University of Kentucky","U.S. Department of Defense","U.S. Department of Defense (United States Department of Defense)","NCI NIH HHS","U.S. Department of Health & Human Services | National Institutes of Health (NIH)","U.S. Department of Health & Human Services | National Institutes of Health","NIGMS NIH HHS"],"pagination":["4190-4204"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12503065"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["44(43)"],"pubmed_abstract":["Although the involvement of polo-like kinase 1 (PLK1) in metabolic reprogramming from oxidative phosphorylation (OXPHOS) to glycolysis has been previously described, the underlying molecular mechanism remains unclear. Pyruvate dehydrogenase (PDH) catalyzes the conversion of pyruvate into acetyl-CoA, the starting material for the tricarboxylic acid (TCA) cycle. In a companion study by Zhang et al., we demonstrated that PLK1 phosphorylation of PDHA1 at threonine 57 (PDHA1-T57) drives its protein degradation via mitophagy activation. Using a stable-isotope resolved metabolomics (SIRM) approach, we now show that PLK1 phosphorylation of PDHA1-T57 results in metabolic reprogramming from OXPHOS to glycolysis. Notably, cells mimicking PDHA1-T57 phosphorylation rely more on the aspartate-malate shu"],"journal":["Oncogene"],"pubmed_title":["PLK1-mediated PDHA1 phosphorylation drives metabolic reprogramming in lung cancer."],"pmcid":["PMC12503065"],"funding_grant_id":["P30CA177558","R01 CA264652","CA157429","P30 GM127211","CA264652","CA256893","DoD-HT9425-24-1-0442","P30 CA177558","R01 CA272483","CA272483","R01 CA256893","R01 CA196634","R01 CA157429","CA196634"],"pubmed_authors":["Liu X","Liu J","Li Z","Wang R","Zhang Y","Rao X","Allison DB","Katz W","Kong Y","Peng J","Zhang Q"],"additional_accession":[]},"is_claimable":false,"name":"PLK1-mediated PDHA1 phosphorylation drives metabolic reprogramming in lung cancer.","description":"Although the involvement of polo-like kinase 1 (PLK1) in metabolic reprogramming from oxidative phosphorylation (OXPHOS) to glycolysis has been previously described, the underlying molecular mechanism remains unclear. Pyruvate dehydrogenase (PDH) catalyzes the conversion of pyruvate into acetyl-CoA, the starting material for the tricarboxylic acid (TCA) cycle. In a companion study by Zhang et al., we demonstrated that PLK1 phosphorylation of PDHA1 at threonine 57 (PDHA1-T57) drives its protein degradation via mitophagy activation. Using a stable-isotope resolved metabolomics (SIRM) approach, we now show that PLK1 phosphorylation of PDHA1-T57 results in metabolic reprogramming from OXPHOS to glycolysis. Notably, cells mimicking PDHA1-T57 phosphorylation rely more on the aspartate-malate shu","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-04T14:49:33.093Z","creation":"2026-05-10T03:11:35.695Z"},"accession":"S-EPMC12503065","cross_references":{"pubmed":["40957950"],"doi":["10.1038/s41388-025-03571-1"]}}