Getting Folded: Chaperone Proteins in Muscle Development, Maintenance and Disease. Issue 9 (September 2014)

• Record Type: Journal Article
• Authors: Smith, Daniel A.; Carland, Carmen R.; Guo, Yiming; Bernstein, Sanford I.
• Is Part Of: Anatomical record. Volume 297:Issue 9(2014:Sep.)
• Page Start: 1637
• Page End: 1649
• Publication Date: 2014-09
• Subjects: Anatomy -- Periodicals; Evolution (Biology) -- Periodicals; Morphology -- Periodicals; 571.3
• DOI: 10.1002/ar.22980
• Languages: English
• ISSNs: 1932-8486

Abstract

<abstract abstract-type="main"> <title>ABSTRACT</title> <p>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. Anat Rec, 297:1637–1649, 2014. © 2014 Wiley Periodicals, Inc.</p> </abstract>