Protein arginine methyltransferases as regulators of cellular stress
- PMID: 39551462
- PMCID: PMC11973959
- DOI: 10.1016/j.expneurol.2024.115060
Protein arginine methyltransferases as regulators of cellular stress
Abstract
Arginine modification can be a "switch" to regulate DNA transcription and a post-translational modification via methylation of a variety of cellular targets involved in signal transduction, gene transcription, DNA repair, and mRNA alterations. This consequently can turn downstream biological effectors "on" and "off". Arginine methylation is catalyzed by protein arginine methyltransferases (PRMTs 1-9) in both the nucleus and cytoplasm, and is thought to be involved in many disease processes. However, PRMTs have not been well-documented in the brain and their function as it relates to metabolism, circulation, functional learning and memory are understudied. In this review, we provide a comprehensive overview of PRMTs relevant to cellular stress, and future directions into PRMTs as therapeutic regulators in brain pathologies.
Keywords: Brain injury; Cellular stress; Neuroinflammation; Protein arginine methyltransferases; Transcription factors.
Copyright © 2024. Published by Elsevier Inc.
Conflict of interest statement
Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Hung Wen Lin reports financial support was provided by National Institute of Health. Mariana Sayuri Berto Udo reports financial support was provided by American Heart Association. Hung Wen Lin reports financial support was provided by American Heart Association. Hung Wen Lin is the honorary treasurer of the International Society for the Study if Fatty Acids and Lipids (ISSFAL) If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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