Precis Future Med.  2019 Dec;3(4):139-145. 10.23838/pfm.2019.00107.

Arginine methylation as a key post-translational modification in skeletal muscle homeostasis: a review

Affiliations
  • 1Department of Molecular Cell Biology, Single Cell Network Research Center, Sungkyunkwan University School of Medicine, Suwon, Korea. nabiya1127@skku.edu

Abstract

Arginine methylation mediated by protein arginine methyltransferases (PRMTs) has emerged as a key post-translational modification of histone or nonhistone substrates. It involves or controls signaling pathways or gene expression implicated in diverse processes, including muscle regeneration and metabolic homeostasis. Reciprocally, loss of skeletal muscle mass and function related to aging or other pathological conditions could be related to the secondary chronic diseases, for example, metabolic syndromes, chronic inflammation, or cardiovascular diseases. Thus, understanding the pathways that regulate muscle homeostasis is critical to develop therapeutic strategies for preventing muscle loss and related secondary chronic diseases. Recent in vivo research using gene-targeting mouse models have advanced our knowledge about the role of several PRMTs in muscle regeneration and metabolic controls. In this review, we will focus on the recent discoveries on the in vivo function of PRMTs in muscle homeostasis.

Keyword

Muscle, skeletal; Regeneration; Metabolism; Protein arginine methyltransferase

MeSH Terms

Aging
Animals
Arginine*
Cardiovascular Diseases
Chronic Disease
Gene Expression
Histones
Homeostasis*
Inflammation
Metabolism
Methylation*
Methyltransferases
Mice
Muscle, Skeletal*
Protein Processing, Post-Translational*
Protein-Arginine N-Methyltransferases
Regeneration
Arginine
Histones
Methyltransferases
Protein-Arginine N-Methyltransferases
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