title: Emerging role for regulated in development and DNA damage 1 (REDD1) in the regulation of skeletal muscle metabolism.
abstract: Since its discovery, the protein regulated in development and DNA damage 1 (REDD1) has been implicated in the cellular response to various stressors. Most notably, its role as a repressor of signaling through the central metabolic regulator, the mechanistic target of rapamycin in complex 1 (mTORC1) has gained considerable attention. Not surprisingly, changes in REDD1 mRNA and protein have been observed in skeletal muscle under various physiological conditions (e.g., nutrient consumption and resistance exercise) and pathological conditions (e.g., sepsis, alcoholism, diabetes, obesity) suggesting a role for REDD1 in regulating mTORC1-dependent skeletal muscle protein metabolism. Our understanding of the causative role of REDD1 in skeletal muscle metabolism is increasing mostly due to the availability of genetically modified mice in which the REDD1 gene is disrupted. Results from such studies provide support for an important role for REDD1 in the regulation of mTORC1 as well as reveal unexplored functions of this protein in relation to other aspects of skeletal muscle metabolism. The goal of this work is to provide a comprehensive review of the role of REDD1 (and its paralog REDD2) in skeletal muscle during both physiological and pathological conditions.
authors.affiliation: Institute of Exercise Physiology and Wellness, The University of Central Florida, Orlando, Florida; bradley.gordon@ucf.edu.
authors.forename: Bradley S
authors.initials: BS
authors.lastname: Gordon
authors.affiliation: Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania; and.
authors.forename: Jennifer L
authors.initials: JL
authors.lastname: Steiner
authors.affiliation: Department of Exercise and Nutrition Sciences, University at Buffalo, Buffalo, New York.
authors.forename: David L
authors.initials: DL
authors.lastname: Williamson
authors.affiliation: Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania; and.
authors.forename: Charles H
authors.initials: CH
authors.lastname: Lang
authors.affiliation: Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania; and.
authors.forename: Scot R
authors.initials: SR
authors.lastname: Kimball
mesh_terms: D000437:Alcoholism / Q000378:metabolism; D000818:Animals; D003920:Diabetes Mellitus / Q000378:metabolism; D015444:Exercise; D006801:Humans; D000076222:Mechanistic Target of Rapamycin Complex 1; D051379:Mice; D046912:Multiprotein Complexes / Q000378:metabolism*; D009124:Muscle Proteins / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism*; D009765:Obesity / Q000378:metabolism; D010805:Physical Conditioning, Animal; D051381:Rats; D012097:Repressor Proteins / Q000378:metabolism / Q000502:physiology; D055070:Resistance Training; D018805:Sepsis / Q000378:metabolism; D058570:TOR Serine-Threonine Kinases / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism* / Q000502:physiology
chemical_list: C469991:DDIT4 protein, human; C469992:Ddit4 protein, mouse; C000632146:Ddit4 protein, rat; D046912:Multiprotein Complexes; D009124:Muscle Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D000076222:Mechanistic Target of Rapamycin Complex 1; D058570:TOR Serine-Threonine Kinases
keywords: DDIT4; RTP801; dig2; muscle mass