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 Lettjournal_title
FEBS lettersauthors
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 Rdoi
10.1016/j.febslet.2013.07.043subject
Has Abstractpub_date
2013-10-01 00:00:00pages
3159-65issue
19eissn
0014-5793issn
1873-3468pii
S0014-5793(13)00572-3journal_volume
587pub_type
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