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Updated: Aug 6, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
Published on: December 16, 2021
Protein arginine methylation and ubiquitination: A prominent crosstalk and its functions in cancer
Jiawen Zhou1,2, Ao Zhang1, Jiuling Zhu1
1Laboratory of Epigenetic Regulation in Molecular Medicine, School of Basic Medical Sciences, Wannan Medical University, Wuhu, Anhui 241002, China.
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.
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