Referenced in: none

Automatically associated channels: Nav1.5

Title: Identification of N-terminal protein acetylation and arginine methylation of the voltage-gated sodium channel in end-stage heart failure human heart.

Authors: Pedro Beltran-Alvarez, Anna Tarradas, Cristina Chiva, Alexandra Pérez-Serra, Montserrat Batlle, Félix Pérez-Villa, Uwe Schulte, Eduard Sabidó, Ramon Brugada, Sara Pagans

Journal, date & volume: J. Mol. Cell. Cardiol., 2014 Nov , 76, 126-9

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/25172307

Abstract
The α subunit of the cardiac voltage-gated sodium channel, NaV1.5, provides the rapid sodium inward current that initiates cardiomyocyte action potentials. Here, we analyzed for the first time the post-translational modifications of NaV1.5 purified from end-stage heart failure human cardiac tissue. We identified R526 methylation as the major post-translational modification of any NaV1.5 arginine or lysine residue. Unexpectedly, we found that the N terminus of NaV1.5 was: 1) devoid of the initiation methionine, and 2) acetylated at the resulting initial alanine residue. This is the first evidence for N-terminal acetylation in any member of the voltage-gated ion channel superfamily. Our results open the door to explore NaV1.5 N-terminal acetylation and arginine methylation levels as drivers or markers of end-stage heart failure.