AI Article Synopsis
- CARM1 is an enzyme that methylates arginine residues on proteins, which plays a role in regulating various processes related to health and disease, particularly in skeletal muscle function.
- The study employed multiple scientific methods to investigate how CARM1 influences muscle stability and adaptability, revealing its importance in muscle homeostasis.
- Findings showed that CARM1 loss led to significant changes in muscle properties and contributed to decreased exercise capacity, highlighting its crucial role in muscle maintenance and remodeling.
Article Abstract
Objective: Coactivator-associated arginine methyltransferase 1 (CARM1) catalyzes the methylation of arginine residues on target proteins to regulate critical processes in health and disease. A mechanistic understanding of the role(s) of CARM1 in skeletal muscle biology is only gradually emerging. The purpose of this study was to elucidate the function of CARM1 in regulating the maintenance and plasticity of skeletal muscle.
Methods: We used transcriptomic, methylproteomic, molecular, functional, and integrative physiological approaches to determine the specific impact of CARM1 in muscle homeostasis.
Results: Our data defines the occurrence of arginine methylation in skeletal muscle and demonstrates that this mark occurs on par with phosphorylation and ubiquitination. CARM1 skeletal muscle-specific knockout (mKO) mice displayed altered transcriptomic and arginine methylproteomic signatures with molecular and functional outcomes confirming remodeled skeletal muscle contractile and neuromuscular junction characteristics, which presaged decreased exercise tolerance. Moreover, CARM1 regulates AMPK-PGC-1α signalling during acute conditions of activity-induced muscle plasticity.
Conclusions: This study uncovers the broad impact of CARM1 in the maintenance and remodelling of skeletal muscle biology.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9379683 | PMC |
| http://dx.doi.org/10.1016/j.molmet.2022.101555 | DOI Listing |
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