title: Dialogue between LKB1 and AMPK: a hot topic at the cellular pole.
abstract: Disruption of cell architecture and change of energy metabolism are two traits of malignant cells. Yet, there was scant evidence that these two cancer hallmarks involved perturbations of a common signaling pathway. Enter LKB1, a kinase that is a tumor suppressor and that is an upstream activator of the adenosine monophosphate (AMP)-activated protein kinase (AMPK), a key sensor of cellular energy status. Four studies now reveal that LKB1 signals through AMPK to facilitate the formation of tight junctions and to maintain epithelial polarity. Thus, LKB1 appears to be a novel class of tumor suppressor that acts as an energy-sensing and polarity checkpoint.
authors: CNRS Unité Mixte de Recherche 5201, Laboratoire de Génétique Moléculaire, Signalisation et Cancer, F-69008 Lyon, France.
authors: Christelle
authors: C
authors: Forcet
authors: Marc
authors: M
authors: Billaud
mesh_terms: D000091162:AMP-Activated Protein Kinase Kinases; D055372:AMP-Activated Protein Kinases; D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry / Q000502:physiology; D033942:Adaptor Proteins, Vesicular Transport / Q000737:chemistry / Q000502:physiology; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D024722:Cardiac Myosins / Q000502:physiology; D016764:Cell Polarity / Q000502:physiology*; D004285:Dogs; D029721:Drosophila Proteins / Q000737:chemistry / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D004331:Drosophila melanogaster / Q000166:cytology / Q000235:genetics / Q000378:metabolism; D004734:Energy Metabolism / Q000502:physiology*; D006801:Humans; D009097:Multienzyme Complexes / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D018994:Myosin Light Chains / Q000502:physiology; D010580:Peutz-Jeghers Syndrome / Q000235:genetics; D010766:Phosphorylation; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology; D019108:Tight Junctions / Q000502:physiology*
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D033942:Adaptor Proteins, Vesicular Transport; D029721:Drosophila Proteins; D009097:Multienzyme Complexes; D018994:Myosin Light Chains; C107184:myosin light chain 2; D000255:Adenosine Triphosphate; D011494:Protein Kinases; C523914:AMPKalpha protein, Drosophila; C495775:LKB1 protein, Drosophila; D017346:Protein Serine-Threonine Kinases; C109790:STK11 protein, human; D000091162:AMP-Activated Protein Kinase Kinases; D055372:AMP-Activated Protein Kinases; D024722:Cardiac Myosins