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Updated: May 9, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
Published on: December 16, 2021
Protein arginine methyl transferases-3 and -5 increase cell surface expression of cardiac sodium channel
Pedro Beltran-Alvarez1, Alexsandra Espejo, Ralf Schmauder
1Cardiovascular Genetics Center, Institut d'Investigació Biomèdica de Girona, Department of Medical Sciences, School of Medicine, University of Girona, 17003 Girona, Spain; Institute for Physiology II, University Hospital, 07743 Jena, Germany.
Abstract:
The α-subunit of the cardiac voltage-gated sodium channel (NaV1.5) 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 NaV1.5 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 NaV1.5 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.
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