ArticleAmerican journal of physiology. Cell physiology2018
Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity.
Article in American journal of physiology. Cell physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 43 citations in OpenAlex.
- Protein arginine methyltransferases coordinate mitochondrial stress adaptation and neuromuscular function.Experimental & molecular medicine · 2026Review
- Gait analysis for functional evaluation in a surgical hindlimb suspension model of muscle atrophy.The Journal of physiology · 2026Article
- Recent advances in the role of CARM1 in skeletal muscle development, metabolism, and homeostasis maintenance.Frontiers in cell and developmental biology · 2025Review
- Epigenetics of Skeletal Muscle Atrophy.International journal of molecular sciences · 2024Review
- Epigenetic control of skeletal muscle atrophy.Cellular & molecular biology letters · 2024Review
- CARM1 drives mitophagy and autophagy flux during fasting-induced skeletal muscle atrophy.Autophagy · 2024Article
- Impact of short-term, pharmacological CARM1 inhibition on skeletal muscle mass, function, and atrophy in mice.American journal of physiology. Endocrinology and metabolism · 2023Article
- PRMT5 links lipid metabolism to contractile function of skeletal muscles.EMBO reports · 2023Article
- Inhibition of type I PRMTs reforms muscle stem cell identity enhancing their therapeutic capacity.eLife · 2023Article
- Arginine Methylation of the PGC-1α C-Terminus Is Temperature-Dependent.Biochemistry · 2023Article
- Role of Pannexin 1 ATP-Permeable Channels in the Regulation of Signaling Pathways during Skeletal Muscle Unloading.International journal of molecular sciences · 2021Article
- A transition to degeneration triggered by oxidative stress in degenerative disorders.Molecular psychiatry · 2021Review
- Role of Protein Arginine Methyltransferases and Inflammation in Muscle Pathophysiology.Frontiers in physiology · 2021Review
- CARM1 Regulates AMPK Signaling in Skeletal Muscle.iScience · 2020Article
- Protein arginine methyltransferase biology in humans during acute and chronic skeletal muscle plasticity.Journal of applied physiology (Bethesda, Md. : 1985) · 2019Article
- Mechanisms of exercise-induced survival motor neuron expression in the skeletal muscle of spinal muscular atrophy-like mice.The Journal of physiology · 2019Article
- Chronic exercise mitigates disease mechanisms and improves muscle function in myotonic dystrophy type 1 mice.The Journal of physiology · 2019Article
- The Role of AMPK in the Regulation of Skeletal Muscle Size, Hypertrophy, and Regeneration.International journal of molecular sciences · 2018Review
- Protein arginine methyltransferase expression and activity during myogenesis.Bioscience reports · 2018Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Protein arginine methyltransferase 1 (PRMT1), PRMT4, and PRMT5 catalyze the methylation of arginine residues on target proteins. Previous work suggests that these enzymes regulate skeletal muscle plasticity. However, the function of PRMTs during disuse-induced muscle remodeling is unknown. The purpose of our study was to determine whether denervation-induced muscle disuse alters PRMT expression and activity in skeletal muscle, as well as to contextualize PRMT biology within the early disuse-evoked events that precede atrophy, which remain largely undefined. Mice were subjected to 6, 12, 24, 72, or 168 h of unilateral hindlimb denervation. Muscle mass decreased by ~30% after 72 or 168 h of neurogenic disuse, depending on muscle fiber type composition. The expression, localization, and activities of PRMT1, PRMT4, and PRMT5 were modified, exhibiting changes in gene expression and activity that were PRMT-specific. Rapid alterations in canonical muscle atrophy signaling such as forkhead box protein O1, muscle RING-finger protein-1, as well as peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α) content, AMP-activated protein kinase (AMPK) and p38 mitogen-activated protein kinase, were observed before measurable decrements in muscle mass. Denervation-induced modifications in AMPK-PRMT1 and PGC-1α-PRMT1 binding revealed a novel, putative PRMT1-AMPK-PGC-1α signaling axis in skeletal muscle. Here, PGC-1α-PRMT1 binding was elevated after 6 h of disuse, whereas AMPK-PRMT1 interactions were reduced following 168 h of denervation. Our data suggest that PRMT biology is integral to the mechanisms that precede and initiate skeletal muscle atrophy during conditions of neurogenic disuse. This study furthers our understanding of the role of PRMTs in governing skeletal muscle plasticity.
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