Referenced in: none

Automatically associated channels: Nav1.5 , TRP

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

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

Journal, date & volume: FEBS Lett., 2013 Oct 1 , 587, 3159-65

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/23912080

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.