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O ‐glycosylation of the cardiac I Ks complex
Author(s) -
Chandrasekhar Kshama D.,
Lvov Anatoli,
Terrenoire Cecile,
Gao Grace Y.,
Kass Robert S.,
Kobertz William R.
Publication year - 2011
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2011.211284
Subject(s) - glycosylation , biogenesis , n linked glycosylation , mutant , glycan , protein subunit , biochemistry , microbiology and biotechnology , chemistry , biology , wild type , glycoprotein , gene
Non‐technical summary Post‐translational modification of cardiac ion channels is a cellular mechanism for maintaining the rhythmicity of the heartbeat. We show that an essential regulatory subunit (KCNE1) of the cardiac I Ks potassium channel complex is glycosylated at threonine‐7 in vivo . Mutations that prevent glycosylation at this amino acid result in cardiac I Ks complexes that are unable to efficiently traffic to the plasma membrane. These results provide a cellular mechanism for a KCNE1 mutation (T7I) that has been associated with cardiac arrhythmias.