Journal article
Charles Brobbey, Liu Liu, Shasha Yin, W. Gan
International Journal of Molecular Sciences, 2022
International Journal of Molecular Sciences, 2022
Semantic Scholar
DOI
PubMedCentral
PubMed
Cite
Cite
APA
Click to copy
Brobbey, C., Liu, L., Yin, S., & Gan, W. (2022). The Role of Protein Arginine Methyltransferases in DNA Damage Response. International Journal of Molecular Sciences.
Chicago/Turabian
Click to copy
Brobbey, Charles, Liu Liu, Shasha Yin, and W. Gan. “The Role of Protein Arginine Methyltransferases in DNA Damage Response.” International Journal of Molecular Sciences (2022).
MLA
Click to copy
Brobbey, Charles, et al. “The Role of Protein Arginine Methyltransferases in DNA Damage Response.” International Journal of Molecular Sciences, 2022.
BibTeX Click to copy
@article{charles2022a,
title = {The Role of Protein Arginine Methyltransferases in DNA Damage Response},
year = {2022},
journal = {International Journal of Molecular Sciences},
author = {Brobbey, Charles and Liu, Liu and Yin, Shasha and Gan, W.}
}
Abstract
In response to DNA damage, cells have developed a sophisticated signaling pathway, consisting of DNA damage sensors, transducers, and effectors, to ensure efficient and proper repair of damaged DNA. During this process, posttranslational modifications (PTMs) are central events that modulate the recruitment, dissociation, and activation of DNA repair proteins at damage sites. Emerging evidence reveals that protein arginine methylation is one of the common PTMs and plays critical roles in DNA damage response. Protein arginine methyltransferases (PRMTs) either directly methylate DNA repair proteins or deposit methylation marks on histones to regulate their transcription, RNA splicing, protein stability, interaction with partners, enzymatic activities, and localization. In this review, we summarize the substrates and roles of each PRMTs in DNA damage response and discuss the synergistic anticancer effects of PRMTs and DNA damage pathway inhibitors, providing insight into the significance of arginine methylation in the maintenance of genome integrity and cancer therapies.
