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

Kim, Hyebeen; Kang, Jong‐Sun; Jeong, Hyun-Ju

doi:10.23838/pfm.2019.00107

Cited by 3 publications

(2 citation statements)

References 23 publications

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“…Alternatively to phosphorylation, FOXO can be regulated by acetylation/deacetylation, methylation and ubiquitination to modulate its activity, localization as well as degradation [ 214 , 215 , 216 ].…”

Section: E3 Ligases Involved In the Regulation Of Muscle Atrophymentioning

confidence: 99%

Ubiquitin Ligases at the Heart of Skeletal Muscle Atrophy Control

et al. 2021

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Skeletal muscle loss is a detrimental side-effect of numerous chronic diseases that dramatically increases mortality and morbidity. The alteration of protein homeostasis is generally due to increased protein breakdown while, protein synthesis may also be down-regulated. The ubiquitin proteasome system (UPS) is a master regulator of skeletal muscle that impacts muscle contractile properties and metabolism through multiple levers like signaling pathways, contractile apparatus degradation, etc. Among the different actors of the UPS, the E3 ubiquitin ligases specifically target key proteins for either degradation or activity modulation, thus controlling both pro-anabolic or pro-catabolic factors. The atrogenes MuRF1/TRIM63 and MAFbx/Atrogin-1 encode for key E3 ligases that target contractile proteins and key actors of protein synthesis respectively. However, several other E3 ligases are involved upstream in the atrophy program, from signal transduction control to modulation of energy balance. Controlling E3 ligases activity is thus a tempting approach for preserving muscle mass. While indirect modulation of E3 ligases may prove beneficial in some situations of muscle atrophy, some drugs directly inhibiting their activity have started to appear. This review summarizes the main signaling pathways involved in muscle atrophy and the E3 ligases implicated, but also the molecules potentially usable for future therapies.

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Section: E3 Ligases Involved In the Regulation Of Muscle Atrophymentioning

confidence: 99%

Ubiquitin Ligases at the Heart of Skeletal Muscle Atrophy Control

et al. 2021

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“…Recent studies have proposed important roles of PRMT7 in muscle regenerative capacity and metabolism ( Kim et al, 2019 ). PRMT7 ablation in satellite cells causes defective muscle regeneration due to premature cellular senescence of satellite cells ( Blanc et al, 2016 ).…”

Section: Protein Arginine Methyltransferasesmentioning

confidence: 99%

Role of Protein Arginine Methyltransferases and Inflammation in Muscle Pathophysiology

Kim

Kang

et al. 2021

Front. Physiol.

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Arginine methylation mediated by protein arginine methyltransferases (PRMTs) is a post-translational modification of both histone and non-histone substrates related to diverse biological processes. PRMTs appear to be critical regulators in skeletal muscle physiology, including regeneration, metabolic homeostasis, and plasticity. Chronic inflammation is commonly associated with the decline of skeletal muscle mass and strength related to aging or chronic diseases, defined as sarcopenia. In turn, declined skeletal muscle mass and strength can exacerbate chronic inflammation. Thus, understanding the molecular regulatory pathway underlying the crosstalk between skeletal muscle function and inflammation might be essential for the intervention of muscle pathophysiology. In this review, we will address the current knowledge on the role of PRMTs in skeletal muscle physiology and pathophysiology with a specific emphasis on its relationship with inflammation.

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Protein Arginine Methyltransferase 1 Ablation in Motor Neurons Causes Mitochondrial Dysfunction Leading to Age-related Motor Neuron Degeneration with Muscle Loss

Kim

Lee

et al. 2023

Research

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Neuromuscular dysfunction is tightly associated with muscle wasting that occurs with age or due to degenerative diseases. However, the molecular mechanisms underlying neuromuscular dysfunction are currently unclear. Recent studies have proposed important roles of Protein arginine methyltransferase 1 (Prmt1) in muscle stem cell function and muscle maintenance. In the current study, we set out to determine the role of Prmt1 in neuromuscular function by generating mice with motor neuron-specific ablation of Prmt1 (mnKO) using Hb9-Cre. mnKO exhibited age-related motor neuron degeneration and neuromuscular dysfunction leading to premature muscle loss and lethality. Prmt1 deficiency also impaired motor function recovery and muscle reinnervation after sciatic nerve injury. The transcriptome analysis of aged mnKO lumbar spinal cords revealed alterations in genes related to inflammation, cell death, oxidative stress, and mitochondria. Consistently, mnKO lumbar spinal cords of sciatic nerve injury model or aged mice exhibited elevated cellular stress response in motor neurons. Furthermore, Prmt1 inhibition in motor neurons elicited mitochondrial dysfunction. Our findings demonstrate that Prmt1 ablation in motor neurons causes age-related motor neuron degeneration attributing to muscle loss. Thus, Prmt1 is a potential target for the prevention or intervention of sarcopenia and neuromuscular dysfunction related to aging.

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

Cited by 3 publications

References 23 publications

Ubiquitin Ligases at the Heart of Skeletal Muscle Atrophy Control

Ubiquitin Ligases at the Heart of Skeletal Muscle Atrophy Control

Role of Protein Arginine Methyltransferases and Inflammation in Muscle Pathophysiology

Protein Arginine Methyltransferase 1 Ablation in Motor Neurons Causes Mitochondrial Dysfunction Leading to Age-related Motor Neuron Degeneration with Muscle Loss

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