title: PKM2 contributes to cancer metabolism.
abstract: Reprogramming of cell metabolism is essential for tumorigenesis, and is regulated by a complex network, in which PKM2 plays a critical role. PKM2 exists as an inactive monomer, less active dimer and active tetramer. While dimeric PKM2 diverts glucose metabolism towards anabolism through aerobic glycolysis, tetrameric PKM2 promotes the flux of glucose-derived carbons for ATP production via oxidative phosphorylation. Equilibrium of the PKM2 dimers and tetramers is critical for tumorigenesis, and is controlled by multiple factors. The PKM2 dimer also promotes aerobic glycolysis by modulating transcriptional regulation. We will discuss the current understanding of PKM2 in regulating cancer metabolism.
authors: Division of Nephrology, Department of Medicine, Hamilton, Ontario, Canada; Division of Urology, Department of Surgery, McMaster University, Hamilton, Ontario, Canada; Father Sean O'Sullivan Research Institute, Hamilton, Ontario, Canada; The Hamilton Center for Kidney Research, St. Joseph's Hospital, Hamilton, Ontario, Canada.
authors: Nicholas
authors: N
authors: Wong
authors: Division of Nephrology, Department of Medicine, Hamilton, Ontario, Canada; Division of Urology, Department of Surgery, McMaster University, Hamilton, Ontario, Canada; Father Sean O'Sullivan Research Institute, Hamilton, Ontario, Canada; The Hamilton Center for Kidney Research, St. Joseph's Hospital, Hamilton, Ontario, Canada.
authors: Diane
authors: D
authors: Ojo
authors: Division of Nephrology, Department of Medicine, Hamilton, Ontario, Canada; Division of Urology, Department of Surgery, McMaster University, Hamilton, Ontario, Canada; Father Sean O'Sullivan Research Institute, Hamilton, Ontario, Canada; The Hamilton Center for Kidney Research, St. Joseph's Hospital, Hamilton, Ontario, Canada.
authors: Judy
authors: J
authors: Yan
authors: Division of Nephrology, Department of Medicine, Hamilton, Ontario, Canada; Division of Urology, Department of Surgery, McMaster University, Hamilton, Ontario, Canada; Father Sean O'Sullivan Research Institute, Hamilton, Ontario, Canada; The Hamilton Center for Kidney Research, St. Joseph's Hospital, Hamilton, Ontario, Canada. Electronic address: damut@mcmaster.ca.
authors: Damu
authors: D
authors: Tang
mesh_terms: D002352:Carrier Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D049109:Cell Proliferation; D002471:Cell Transformation, Neoplastic / Q000473:pathology; D015972:Gene Expression Regulation, Neoplastic; D005947:Glucose / Q000378:metabolism; D006019:Glycolysis / Q000502:physiology*; D006801:Humans; D051795:Hypoxia-Inducible Factor 1, alpha Subunit / Q000378:metabolism; D008565:Membrane Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism; D013963:Thyroid Hormones / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D000097810:Thyroid Hormone-Binding Proteins
chemical_list: D002352:Carrier Proteins; D005947:Glucose; D051795:Hypoxia-Inducible Factor 1, alpha Subunit; D008565:Membrane Proteins; D009363:Neoplasm Proteins; D016271:Proto-Oncogene Proteins c-myc; D013963:Thyroid Hormones; D000097810:Thyroid Hormone-Binding Proteins; C497442:HIF1A protein, human; C489427:MYC protein, human
keywords: Aerobic glycolysis; Cancer metabolism; Cell signalling; PKM2