Interaction Between KCNQ1 Gain-of-Function Residues
نویسندگان
چکیده
منابع مشابه
KCNQ1 gain-of-function mutation in familial atrial fibrillation.
Atrial fibrillation (AF) is a common cardiac arrhythmia whose molecular etiology is poorly understood. We studied a family with hereditary persistent AF and identified the causative mutation (S140G) in the KCNQ1 (KvLQT1) gene on chromosome 11p15.5. The KCNQ1 gene encodes the pore-forming alpha subunit of the cardiac I(Ks) channel (KCNQ1/KCNE1), the KCNQ1/KCNE2 and the KCNQ1/KCNE3 potassium chan...
متن کاملIdentification of a protein–protein interaction between KCNE1 and the activation gate machinery of KCNQ1
KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K(+) channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein-protein interaction between the KCNE1 C-terminal domain...
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15 صفحه اولKCNQ1 assembly and function is blocked by long-QT syndrome mutations that disrupt interaction with calmodulin.
Calmodulin (CaM) has been recognized as an obligate subunit for many ion channels in which its function has not been clearly established. Because channel subunits associate early during channel biosynthesis, CaM may provide a mechanism for Ca(2+)-dependent regulation of channel formation. Here we show that CaM is a constitutive component of KCNQ1 K+ channels, the most commonly mutated long-QT s...
متن کاملIdentification of specific pore residues mediating KCNQ1 inactivation. A novel mechanism for long QT syndrome.
KCNQ1 inactivation bears electrophysiological characteristics different from classical N- and C-type inactivation in Shaker-like potassium channels. However, the molecular site of KCNQ1 inactivation has not yet been determined. KCNQ2 channels do not exert a fast inactivation in contrast to KCNQ1 channels. By expressing functional chimeras between KCNQ1 and KCNQ2 in Xenopus oocytes, we mapped th...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2014
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2013.11.818