title: Protein arginylation, a global biological regulator that targets actin cytoskeleton and the muscle.
abstract: Posttranslational addition of Arg to proteins, mediated by arginyltransferase ATE1 has been first observed in 1963 and remained poorly understood for decades since its original discovery. Recent work demonstrated the global nature of arginylation and its essential role in multiple physiological pathways during embryogenesis and adulthood and identified over a hundred of proteins arginylated in vivo. Among these proteins, the prominent role belongs to the actin cytoskeleton and the muscle, and follow up studies strongly suggests that arginylation constitutes a novel biological regulator of contractility. This review presents an overview of the studies of protein arginylation that led to the discovery of its major role in the muscle.
authors.affiliation: Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania.
authors.forename: Anna
authors.initials: A
authors.lastname: Kashina
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism*; D019881:Aminoacyltransferases / Q000378:metabolism*; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D006801:Humans; D009119:Muscle Contraction; D009124:Muscle Proteins / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction
chemical_list: D009124:Muscle Proteins; D001120:Arginine; D019881:Aminoacyltransferases; C019727:arginyltransferase
keywords: actin; arginylation; muscle