©The Author(s) 2023. Published by Baishideng Publishing Group Inc. All rights reserved.
World J Biol Chem. Oct 17, 2023; 14(5): 84-98
Published online Oct 17, 2023. doi: 10.4331/wjbc.v14.i5.84
Published online Oct 17, 2023. doi: 10.4331/wjbc.v14.i5.84
Protein arginine methyltransferase 6 is a novel substrate of protein arginine methyltransferase 1
Meng-Tong Cao, You Feng, Y George Zheng, Department of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, GA 30602, United States
Author contributions: Cao MT, Feng Y and Zheng YG designed the research study; Cao MT and Feng Y performed the experiments; All authors analyzed the data, wrote the manuscript, and have read and approve the final manuscript.
Supported by National Institutes of Health , No. 5R01GM126154 and No. 1R35GM149230 .
Institutional review board statement: The study was reviewed and approved by the University of Georgia Institutional Biosafety Committee protocol number.
Conflict-of-interest statement: We have no financial relationships to disclose.
Data sharing statement: No additional data are available.
Corresponding author: Y George Zheng, PhD, Professor, Department of Pharmaceutical and Biomedical Sciences, University of Georgia, No. 250 W. Green St., Athens, GA 30602, United States. yzheng@uga.edu
Received: July 19, 2023
Peer-review started: July 19, 2023
First decision: August 31, 2023
Revised: September 8, 2023
Accepted: September 26, 2023
Article in press: September 26, 2023
Published online: October 17, 2023
Processing time: 85 Days and 18 Hours
Peer-review started: July 19, 2023
First decision: August 31, 2023
Revised: September 8, 2023
Accepted: September 26, 2023
Article in press: September 26, 2023
Published online: October 17, 2023
Processing time: 85 Days and 18 Hours
Core Tip
Core Tip: We reported the interplay between protein arginine methyltransferase (PRMT) 1 and PRMT6, and PRMT6 is a substrate of PRMT1. The major methylation site in PRMT6 is R106 for PRMT1 catalysis and the methylation by PRMT1 regulates the enzymatic activity of PRMT6. This study is important for understanding the cross-talking relationship between PRMTs.