title: Mitochondrial protein phosphorylation as a regulatory modality: implications for mitochondrial dysfunction in heart failure.
abstract: Phosphorylation of mitochondrial proteins has been recognized for decades, and the regulation of pyruvate- and branched-chain α-ketoacid dehydrogenases by an atypical kinase/phosphatase cascade is well established. More recently, the development of new mass spectrometry-based technologies has led to the discovery of many novel phosphorylation sites on a variety of mitochondrial targets. The evidence suggests that the major classes of kinase and several phosphatases may be present at the mitochondrial outer membrane, intermembrane space, inner membrane, and matrix, but many questions remain to be answered as to the location, timing, and reversibility of these phosphorylation events and whether they are functionally relevant. The authors review phosphorylation as a mitochondrial regulatory strategy and highlight its possible role in the pathophysiology of cardiac hypertrophy and failure.
authors: Department of Medicine, Division of Cardiology, The Johns Hopkins University, Baltimore, MD 21205-2195, USA. bor@jhmi.edu
authors: Brian
authors: B
authors: O'Rourke
authors: Jennifer E
authors: JE
authors: Van Eyk
authors: D Brian
authors: DB
authors: Foster
mesh_terms: D000818:Animals; D004734:Energy Metabolism / Q000502:physiology*; D006333:Heart Failure / Q000378:metabolism*; D006801:Humans; D008929:Mitochondria, Heart / Q000502:physiology*; D051336:Mitochondrial Membranes / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D018384:Oxidative Stress; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*
chemical_list: D024101:Mitochondrial Proteins; D009097:Multienzyme Complexes; D011494:Protein Kinases