Review
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World J Biol Chem. May 26, 2014; 5(2): 115-129
Published online May 26, 2014. doi: 10.4331/wjbc.v5.i2.115
Role of PRMTs in cancer: Could minor isoforms be leaving a mark?
R Mitchell Baldwin, Alan Morettin, Jocelyn Côté
R Mitchell Baldwin, Alan Morettin, Jocelyn Côté, Department of Cellular and Molecular Medicine, Rm. 3111a, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada
Author contributions: Baldwin RM and Côté J wrote the manuscript; Baldwin RM, Côté J and Morettin A contributed to the editing and critical assessment of the manuscript.
Supported by Cancer projects in the Côté lab are funded through the Cancer Research Society, Canadian Research Institutes of Health Research and Canadian Breast Cancer Foundation
Correspondence to: Jocelyn Côté, PhD, Associate Professor, Department of Cellular and Molecular Medicine, Rm. 3111a, Faculty of Medicine, University of Ottawa, 451 Smyth Road, Ottawa, ON K1H 8M5, Canada. jcote@uottawa.ca
Telephone: +1-613-5625800-8660 Fax: +1-613-5625434
Received: November 30, 2013
Revised: March 5, 2014
Accepted: April 17, 2014
Published online: May 26, 2014
Processing time: 192 Days and 24 Hours
Core Tip

Core tip: This review focuses on the current knowledge regarding alternative protein arginine methyltransferases (PRMT) isoforms and evidence supporting their potential impact in cancer. Alternative PRMT isoforms have been identified for PRMT1, PRMT2, CARM1 and PRMT7 and more may exist for the other PRMT family members. The presence of these isoforms adds a layer of complexity to the functional roles PRMTs play in normal and disease contexts. These alternative isoforms have unique characteristics that may offer clarification to conflicting roles documented in the literature. Finally, understanding the specific functions of these isoforms is crucial for fully characterizing the therapeutic potential of PRMTs in cancer.