O ‐glycosylation of the cardiac I Ks  complex | Zendy

Chandrasekhar Kshama D. | Zendy; Lvov Anatoli | Zendy; Terrenoire Cecile | Zendy; Gao Grace Y. | Zendy; Kass Robert S. | Zendy; Kobertz William R. | Zendy

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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.

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