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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Beltran-Alvarez P,Espejo A,Schmauder R,Beltran C,Mrowka R,Linke T,Batlle M,Pérez-Villa F,Pérez GJ,Scornik FS,Benndorf K,Pagans S,Zimmer T,Brugada R

doi

10.1016/j.febslet.2013.07.043

subject

Has Abstract

pub_date

2013-10-01 00:00:00

pages

3159-65

issue

19

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(13)00572-3

journal_volume

587

pub_type

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