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Protein arginine methyl transferases‐3 and ‐5 increase cell surface expression of cardiac sodium channel
Author(s) -
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
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.07.043
Subject(s) - arginine , methylation , hek 293 cells , sodium channel , chemistry , sodium , enzyme , potassium channel , protein subunit , biochemistry , biophysics , biology , amino acid , gene , organic chemistry
The α‐subunit of the cardiac voltage‐gated sodium channel (Na V 1.5) plays a central role in cardiomyocyte excitability. We have recently reported that Na V 1.5 is post‐translationally modified by arginine methylation. Here, we aimed to identify the enzymes that methylate Na V 1.5, and to describe the role of arginine methylation on Na V 1.5 function. Our results show that protein arginine methyl transferase (PRMT)‐3 and ‐5 methylate Na V 1.5 in vitro, interact with Na V 1.5 in human embryonic kidney (HEK) cells, and increase Na V 1.5 current density by enhancing Na V 1.5 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.