title: Getting folded: chaperone proteins in muscle development, maintenance and disease.
abstract: Chaperone proteins are critical for protein folding and stability, and hence are necessary for normal cellular organization and function. Recent studies have begun to interrogate the role of this specialized class of proteins in muscle biology. During development, chaperone-mediated folding of client proteins enables their integration into nascent functional sarcomeres. In addition to assisting with muscle differentiation, chaperones play a key role in the maintenance of muscle tissues. Furthermore, disruption of the chaperone network can result in neuromuscular disease. In this review, we discuss how chaperones are involved in myofibrillogenesis, sarcomere maintenance, and muscle disorders. We also consider the possibilities of therapeutically targeting chaperones to treat muscle disease.
authors.affiliation: Department of Biology, The Molecular Biology Institute, San Diego State University, San Diego, California.
authors.forename: Daniel A
authors.initials: DA
authors.lastname: Smith
authors.forename: Carmen R
authors.initials: CR
authors.lastname: Carland
authors.forename: Yiming
authors.initials: Y
authors.lastname: Guo
authors.forename: Sanford I
authors.initials: SI
authors.lastname: Bernstein
mesh_terms: D000818:Animals; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D009119:Muscle Contraction; D024510:Muscle Development; D009124:Muscle Proteins / Q000737:chemistry / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D009135:Muscular Diseases / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D017510:Protein Folding; D015398:Signal Transduction; D013329:Structure-Activity Relationship
chemical_list: D018832:Molecular Chaperones; D009124:Muscle Proteins
keywords: chaperones; contractile proteins; myofibril; protein folding; sarcomere