ArticleChannels (Austin, Tex.)
KCNQ1/KCNE1 assembly, co-translation not required.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Functional Profiling ofCirculation. Genomic and precision medicine · 2025Article
- Calmodulin-dependent KCNE4 dimerization controls membrane targeting.Scientific reports · 2021Article
- Delayed KCNQ1/KCNE1 assembly on the cell surface helps IThe Journal of physiology · 2021Article
- Article
- Mechanisms of KCNQ1 channel dysfunction in long QT syndrome involving voltage sensor domain mutations.Science advances · 2018Article
- Adult Ventricular Myocytes Segregate KCNQ1 and KCNE1 to Keep theCirculation. Arrhythmia and electrophysiology · 2017Article
- Structural basis for KCNE3 modulation of potassium recycling in epithelia.Science advances · 2016Article
- Structural investigation of the transmembrane domain of KCNE1 in proteoliposomes.Biochemistry · 2014Article
- Ion channels and schizophrenia: a gene set-based analytic approach to GWAS data for biological hypothesis testing.Human genetics · 2012Article
- Disruption of kv1.3 channel forward vesicular trafficking by hypoxia in human T lymphocytes.The Journal of biological chemistry · 2012Article
- KCNE Regulation of K(+) Channel Trafficking - a Sisyphean Task?Frontiers in physiology · 2012Article
- Neuromodulation independently determines correlated channel expression and conductance levels in motor neurons of the stomatogastric ganglion.Journal of neurophysiology · 2012Article
- KV7 channelopathies.Pflugers Archiv : European journal of physiology · 2010Review
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Voltage-gated potassium channels are often assembled with accessory proteins that increase their functional diversity. KCNE proteins are small accessory proteins that modulate voltage-gated potassium (K(V)) channels. Although the functional effects of various KCNE proteins have been described, many questions remain regarding their assembly with the pore-forming subunits. For example, while previous experiments with some K(V) channels suggest that the association of the pore-subunit with the accessory subunits occurs co-translationally in the endoplasmic reticulum, it is not known whether KCNQ1 assembly with KCNE1 occurs in a similar manner to generate the medically important cardiac slow delayed rectifier current (I(Ks)). In this study we used a novel approach to demonstrate that purified recombinant human KCNE1 protein (prKCNE1) modulates KCNQ1 channels heterologously expressed in Xenopus oocytes resulting in generation of I(Ks). Incubation of KCNQ1-expressing oocytes with cycloheximide did not prevent I(Ks) expression following prKCNE1 injection. By contrast, incubation with brefeldin A prevented KCNQ1 modulation by prKCNE1. Moreover, injection of the trafficking-deficient KCNE1-L51H reduced KCNQ1 currents. Together, these observations indicate that while assembly of KCNE1 with KCNQ1 does not require co-translation, functional KCNQ1-prKCNE1 channels assemble early in the secretory pathway and reach the plasma membrane via vesicular trafficking.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.