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

Anat Rec (Hoboken). 2014 Sep;297(9):1637-49. doi: 10.1002/ar.22980.

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.

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

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Humans
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism*
  • Molecular Structure
  • Muscle Contraction
  • Muscle Development
  • Muscle Proteins / chemistry
  • Muscle Proteins / metabolism*
  • Muscles / metabolism*
  • Muscles / pathology
  • Muscles / physiopathology
  • Muscular Diseases / metabolism*
  • Muscular Diseases / pathology
  • Muscular Diseases / physiopathology
  • Protein Folding*
  • Signal Transduction
  • Structure-Activity Relationship

Substances

  • Molecular Chaperones
  • Muscle Proteins