| Literature DB >> 25125177 |
Daniel A Smith1, Carmen R Carland, Yiming Guo, Sanford I Bernstein.
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.Entities:
Keywords: chaperones; contractile proteins; myofibril; protein folding; sarcomere
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Year: 2014 PMID: 25125177 PMCID: PMC4135391 DOI: 10.1002/ar.22980
Source DB: PubMed Journal: Anat Rec (Hoboken) ISSN: 1932-8486 Impact factor: 2.064