ReviewFrontiers in physiology2017
Regulation of Skeletal Muscle Plasticity by Protein Arginine Methyltransferases and Their Potential Roles in Neuromuscular Disorders.
Review in Frontiers in physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 51 citations in OpenAlex.
- Protein arginine methyltransferases as metabolic regulators: many roles beyond cancer.Science China. Life sciences · 2026Review
- Discovery of novel PRMT1 inhibitors: a combined approach using AI classification model and traditional virtual screening.Frontiers in chemistry · 2025Article
- Epigenetic control of skeletal muscle atrophy.Cellular & molecular biology letters · 2024Review
- Protein arginine methyltransferase 2 controls inflammatory signaling in acute myeloid leukemia.Communications biology · 2024Article
- CARM1 drives mitophagy and autophagy flux during fasting-induced skeletal muscle atrophy.Autophagy · 2024Article
- Metabolomics of cerebrospinal fluid reveals candidate diagnostic biomarkers to distinguish between spinal muscular atrophy type II and type III.CNS neuroscience & therapeutics · 2024Article
- PRMT5 mediates FoxO1 methylation and subcellular localization to regulate lipophagy in myogenic progenitors.Cell reports · 2023Article
- Anoikis resistance and immune escape mediated by Epstein-Barr virus-encoded latent membrane protein 1-induced stabilization of PGC-1α promotes invasion and metastasis of nasopharyngeal carcinoma.Journal of experimental & clinical cancer research : CR · 2023Article
- Functional Implications of Protein Arginine Methyltransferases (PRMTs) in Neurodegenerative Diseases.Biology · 2023Review
- Reduced C9orf72 expression exacerbates polyGR toxicity in patient iPSC-derived motor neurons and a Type I protein arginine methyltransferase inhibitor reduces that toxicity.Frontiers in cellular neuroscience · 2023Article
- Review
- Role of Protein Arginine Methyltransferases and Inflammation in Muscle Pathophysiology.Frontiers in physiology · 2021Review
- Hypothesis and Theory: Roles of Arginine Methylation in C9orf72-Mediated ALS and FTD.Frontiers in cellular neuroscience · 2021Article
- CARM1 Regulates AMPK Signaling in Skeletal Muscle.iScience · 2020Article
- Calycosin inhibited autophagy and oxidative stress in chronic kidney disease skeletal muscle atrophy by regulating AMPK/SKP2/CARM1 signalling pathway.Journal of cellular and molecular medicine · 2020Article
- Article
- Posttranslational regulation of PGC-1α and its implication in cancer metabolism.International journal of cancer · 2019Review
- Protein arginine methyltransferase biology in humans during acute and chronic skeletal muscle plasticity.Journal of applied physiology (Bethesda, Md. : 1985) · 2019Article
- PRMTs and miRNAs: functional cooperation in cancer and beyond.Cell cycle (Georgetown, Tex.) · 2019Review
- Protein arginine methyltransferase expression and activity during myogenesis.Bioscience reports · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze the methylation of arginine residues on target proteins, thereby mediating a diverse set of intracellular functions that are indispensable for survival. Indeed, full-body knockouts of specific PRMTs are lethal and PRMT dysregulation has been implicated in the most prevalent chronic disorders, such as cancers and cardiovascular disease (CVD). PRMTs are now emerging as important mediators of skeletal muscle phenotype and plasticity. Since their first description in muscle in 2002, a number of studies employing wide varieties of experimental models support the hypothesis that PRMTs regulate multiple aspects of skeletal muscle biology, including development and regeneration, glucose metabolism, as well as oxidative metabolism. Furthermore, investigations in non-muscle cell types strongly suggest that proteins, such as peroxisome proliferator-activated receptor-γ coactivator-1α, E2F transcription factor 1, receptor interacting protein 140, and the tumor suppressor protein p53, are putative downstream targets of PRMTs that regulate muscle phenotype determination and remodeling. Recent studies demonstrating that PRMT function is dysregulated in Duchenne muscular dystrophy (DMD), spinal muscular atrophy (SMA), and amyotrophic lateral sclerosis (ALS) suggests that altering PRMT expression and/or activity may have therapeutic value for neuromuscular disorders (NMDs). This review summarizes our understanding of PRMT biology in skeletal muscle, and identifies uncharted areas that warrant further investigation in this rapidly expanding field of research.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.