Protein arginine methyl transferases-3 and -5 increase cell surface expression of cardiac sodium channel

Beltran-Alvarez, Pedro; Espejo, Alexsandra; Schmauder, Ralf; Beltran, Carlos; Mrowka, Ralf; Linke, Thomas; Batlle, Montserrat; Pérez-Villa, Félix; Pérez, Guillermo J.; Scornik, Fabiana S.; Benndorf, Klaus; Pagans, Sara; Zimmer, Thomas; Brugada, Ramon

Abstract

The α-subunit of the cardiac voltage-gated sodium channel (Na V1.5) plays a central role in cardiomyocyte excitability. We have recently reported that NaV1.5 is post-translationally modified by arginine methylation. Here, we aimed to identify the enzymes that methylate NaV1.5, and to describe the role of arginine methylation on Na V1.5 function. Our results show that protein arginine methyl transferase (PRMT)-3 and -5 methylate NaV1.5 in vitro, interact with NaV1.5 in human embryonic kidney (HEK) cells, and increase Na V1.5 current density by enhancing NaV1.5 cell surface expression. Our observations are the first evidence of regulation of a voltage-gated ion channel, including calcium, potassium, sodium and TRP channels, by arginine methylation. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Beltran-Alvarez, P., Espejo, A., Schmauder, R., Beltran, C., Mrowka, R., Linke, T., …Brugada, R. (2013). Protein arginine methyl transferases-3 and -5 increase cell surface expression of cardiac sodium channel. FEBS Letters, 587(19), 3159-3165. https://doi.org/10.1016/j.febslet.2013.07.043

• Journal Article Type: Article
• Acceptance Date: Jul 16, 2013
• Online Publication Date: Jul 31, 2013
• Publication Date: Oct 1, 2013
• Deposit Date: Apr 1, 2022
• Journal: FEBS Letters
• Print ISSN: 0014-5793
• Electronic ISSN: 1873-3468
• Publisher: Wiley
• Peer Reviewed: Peer Reviewed
• Volume: 587
• Issue: 19
• Pages: 3159-3165
• DOI: https://doi.org/10.1016/j.febslet.2013.07.043
• Public URL: https://hull-repository.worktribe.com/output/3570068