Ubiquitin Ligases in Longevity and Aging Skeletal Muscle
Document Type
Article
Publication Date
7-9-2022
Subject Area
Longevity; Muscle, Skeletal (metabolism); Proteasome Endopeptidase Complex (metabolism); Quality of Life; Ubiquitin (metabolism); Ubiquitin-Protein Ligases (metabolism)
Abstract
The development and prevalence of diseases associated with aging presents a global health burden on society. One hallmark of aging is the loss of proteostasis which is caused in part by alterations to the ubiquitin-proteasome system (UPS) and lysosome-autophagy system leading to impaired function and maintenance of mass in tissues such as skeletal muscle. In the instance of skeletal muscle, the impairment of function occurs early in the aging process and is dependent on proteostatic mechanisms. The UPS plays a pivotal role in degradation of misfolded and aggregated proteins. For the purpose of this review, we will discuss the role of the UPS system in the context of age-related loss of muscle mass and function. We highlight the significant role that E3 ubiquitin ligases play in the turnover of key components (e.g., mitochondria and neuromuscular junction) essential to skeletal muscle function and the influence of aging. In addition, we will briefly discuss the contribution of the UPS system to lifespan. By understanding the UPS system as part of the proteostasis network in age-related diseases and disorders such as sarcopenia, new discoveries can be made and new interventions can be developed which will preserve muscle function and maintain quality of life with advancing age.
Publication Title
International journal of molecular sciences
Volume
23
Issue
14
Digital Object Identifier (DOI)
10.3390/ijms23147602
PubMed ID
35886949
E-ISSN
1422-0067
Language
eng
Citation Information
Hughes, David C.; Baehr, Leslie M.; Waddell, David S.; Sharples, Adam P.; and Bodine, Sue C., "Ubiquitin Ligases in Longevity and Aging Skeletal Muscle" (2022). UNF Faculty Research and Scholarship. 3204.
https://digitalcommons.unf.edu/unf_faculty_publications/3204