Protein arginine methylation and ubiquitination: A prominent crosstalk and its functions in cancer.

Authors

Jiawen Zhou, Ao Zhang, Jiuling Zhu, Fei Tang, Ziyang Yuan, Wenlong Ma, Qi Wang, Jun Lu, Shu Li, Zhongwei Li

Published in

Genes & diseases. Volume 13. Issue 6. Pages 101997. Epub Dec 19, 2025.

Abstract

Protein arginine methyltransferases (PRMTs) catalyze the formation of arginine methylations in histones and nonhistone proteins. PRMT family members strongly affect the malignant progression of cancer. Recently, an increasing number of studies have shown that the interactions of protein arginine methylation and ubiquitination play crucial roles in various essential biological processes related to cancer, such as the DNA damage response (DDR), protein stability, immune escape and signal transduction, which significantly influence cancer progression. This article presents an overview of the mechanisms by which the crosstalk between arginine methylation and ubiquitination impacts cancer. Moreover, we explore future research directions related to arginine methylation and ubiquitination crosstalk in cancer treatment. The goal is to provide a theoretical foundation and potential applications for related basic research and the development of anticancer drugs.

PMID:
42502485
Bibliographic data and abstract were imported from PubMed on 26 Jul 2026.

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