Literature DB >> 25125177

Getting folded: chaperone proteins in muscle development, maintenance and disease.

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.
© 2014 Wiley Periodicals, Inc.

Entities:  

Keywords:  chaperones; contractile proteins; myofibril; protein folding; sarcomere

Mesh:

Substances:

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


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