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

DA Smith, CR Carland, Y Guo… - The Anatomical …, 2014 - Wiley Online Library
DA Smith, CR Carland, Y Guo, SI Bernstein
The Anatomical Record, 2014Wiley Online Library
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 …
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. Anat Rec, 297:1637–1649, 2014. © 2014 Wiley Periodicals, Inc.
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