Next Article in Journal
Antiangiogenic Effect of Flavonoids and Chalcones: An Update
Next Article in Special Issue
Physicochemical Properties of the Mammalian Molecular Chaperone HSP60
Previous Article in Journal
Transcriptome Analysis of Tomato Leaf Spot Pathogen Fusarium proliferatum: De novo Assembly, Expression Profiling, and Identification of Candidate Effectors
Previous Article in Special Issue
Heat Shock Proteins in Vascular Diabetic Complications: Review and Future Perspective
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessReview
Int. J. Mol. Sci. 2018, 19(1), 32; https://doi.org/10.3390/ijms19010032

Chaperones and the Proteasome System: Regulating the Construction and Demolition of Striated Muscle

Department of Biological Sciences, University of Alberta, Edmonton, AB T6G 2E9, Canada
*
Author to whom correspondence should be addressed.
Received: 21 October 2017 / Revised: 28 November 2017 / Accepted: 18 December 2017 / Published: 22 December 2017
(This article belongs to the Special Issue Molecular Chaperones)
View Full-Text   |   Download PDF [6670 KB, uploaded 23 December 2017]   |  

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. View Full-Text
Keywords: molecular chaperone; misfolded protein; protein degradation; protein complex assembly; homeostasis; HSP; sarcomere molecular chaperone; misfolded protein; protein degradation; protein complex assembly; homeostasis; HSP; sarcomere
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Carlisle, C.; Prill, K.; Pilgrim, D. Chaperones and the Proteasome System: Regulating the Construction and Demolition of Striated Muscle. Int. J. Mol. Sci. 2018, 19, 32.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top