Abstract
Protein folding factors (chaperones) are required for many diverse cellular functions. In striated muscle, chaperones are required for contractile protein function, as well as the larger scale assembly of the basic unit of muscle, the sarcomere. The sarcomere is complex and composed of hundreds of proteins and the number of proteins and processes recognized to be regulated by chaperones has increased dramatically over the past decade. Research in the past ten years has begun to discover and characterize the chaperones involved in the assembly of the sarcomere at a rapid rate. Because of the dynamic nature of muscle, wear and tear damage is inevitable. Several systems, including chaperones and the ubiquitin proteasome system (UPS), have evolved to regulate protein turnover. Much of our knowledge of muscle development focuses on the formation of the sarcomere but recent work has begun to elucidate the requirement and role of chaperones and the UPS in sarcomere maintenance and disease. This review will cover the roles of chaperones in sarcomere assembly, the importance of chaperone homeostasis and the cooperation of chaperones and the UPS in sarcomere integrity and disease.
Highlights
The unique tertiary and quaternary structure of a protein is critical for its function
One of the purposes of this review is to highlight our current knowledge of the roles of chaperone and ubiquitin proteasome system (UPS) related responses in striated muscle with respect to what has been studied in other organ systems
The client protein is degraded by the proteasome, an enzyme composed of a 20S catalytic core and one 19S regulatory cap, forming the 26S proteasome, or two 19S regulatory caps, forming the 30S proteasome [50,51] UPS mediated degradation occurs through the 26S proteasome in striated muscle
Summary
The unique tertiary and quaternary structure of a protein is critical for its function. A new layer of complexity is added to this process as protein homeostasis (proteostasis) must occur as the tissue moves Striated muscle exemplifies this complexity, as hundreds of components must be properly synthesized, folded and incorporated into its basic contractile unit, the sarcomere, for the tissue to function. The client protein is degraded by the proteasome, an enzyme composed of a 20S catalytic core and one 19S regulatory cap, forming the 26S proteasome, or two 19S regulatory caps, forming the 30S proteasome [50,51] UPS mediated degradation occurs through the 26S proteasome in striated muscle. We will discuss known muscle chaperones, with specific focus on their regulation and interaction with the UPS and the roles of both in client protein homeostasis during sarcomere assembly and maintenance.
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