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The PTEN tumor suppressor is frequently mutated or deleted in cancer and regulates glucose metabolism through the PI3K-AKT pathway. However, whether PTEN directly regulates glycolysis in tumor cells is unclear. We demonstrate here that PTEN directly interacts with phosphoglycerate kinase 1 (PGK1). PGK1 functions not only as a glycolytic enzyme but also as a protein kinase intermolecularly autophosphorylating itself at Y324 for activation. The protein phosphatase activity of PTEN dephosphorylates and inhibits autophosphorylated PGK1, thereby inhibiting glycolysis, ATP production, and brain tumor cell proliferation. In addition, knockin expression of a PGK1 Y324F mutant inhibits brain tumor formation. Analyses of human glioblastoma specimens reveals that PGK1 Y324 phosphorylation levels inversely correlate with PTEN expression status and are positively associated with poor prognosis in glioblastoma patients. This work highlights the instrumental role of PGK1 autophosphorylation in its activation and PTEN protein phosphatase activity in governing glycolysis and tumorigenesis.
Pubmed ID: 31492635
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Commercial provider of software solutions for drug discovery applications offering tools, services, and research collaborations. The software portfolio ranges from design, over screening, to the visualization of ligand libraries, for hit identification, optimization, and scaffold hopping. With a stellar scientific advisory board and founders from academia who intensely collaborate with pharma, BioSolveIT catalyzes products off of university research successes with proven pharmaceutical industry application. They provide software products within the areas of ligand and structure-based drug design and is the pioneer of computational fragment-based ligand design. BioSolveIT innovate break-throughs in drug discovery by supplying smooth, user-centered designed tools bringing different researchers together for efficient multidisciplinary drug design.
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