Protein arginine methylation of non-histone proteins and its role in diseases |
| |
| Authors: | Han Wei Rasika Mundade Kevin Lange |
| |
| Affiliation: | 1. Department of Pharmacology and Toxicology;2. Indiana University School of Medicine;3. Indianapolis, IN USA;4. Department of Biochemistry and Molecular Biology |
| |
| Abstract: | Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate arginine residues on histones and other proteins. PRMTs play a crucial role in influencing various cellular functions, including cellular development and tumorigenesis. Arginine methylation by PRMTs is found on both nuclear and cytoplasmic proteins. Recently, there is increasing evidence regarding post-translational modifications of non-histone proteins by PRMTs, illustrating the previously unknown importance of PRMTs in the regulation of various cellular functions by post-translational modifications. In this review, we present the recent developments in the regulation of non-histone proteins by PRMTs. |
| |
| Keywords: | post-translational modification arginine protein arginine methyltransferases |
|
