ArticleThe Journal of physiology2011
O-glycosylation of the cardiac I(Ks) complex.
Article in The Journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed.
- Molecular Epidemiology of Human Metapneumovirus Infections in Children from San Luis Potosí-Mexico.Viruses · 2025Article
- Article
- Quantification and Site-Specific Analysis of Co-occupied N- and O-Glycopeptides.Journal of proteome research · 2024Article
- Protein glycosylation in cardiovascular health and disease.Nature reviews. Cardiology · 2024Review
- Quantification and site-specific analysis of co-occupied N- and O-glycopeptides.bioRxiv : the preprint server for biology · 2024Article
- High-throughput functional mapping of variants in an arrhythmia gene, KCNE1, reveals novel biology.Genome medicine · 2024Article
- Modulation of IJournal of cellular physiology · 2022Article
- Delayed KCNQ1/KCNE1 assembly on the cell surface helps IThe Journal of physiology · 2021Article
- An Overview of Glycosylation and its Impact on Cardiovascular Health and Disease.Frontiers in molecular biosciences · 2021Review
- Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021Article
- Article
- Mutational and phenotypic spectra of KCNE1 deficiency in Jervell and Lange-Nielsen Syndrome and Romano-Ward Syndrome.Human mutation · 2019Article
- Chronic in vivo angiotensin II administration differentially modulates the slow delayed rectifier channels in atrial and ventricular myocytes.Heart rhythm · 2019Article
- Sialic acids attached to N- and O-glycans within the Nav1.4 D1S5-S6 linker contribute to channel gating.Biochimica et biophysica acta · 2015Article
- Hydrogen peroxide induces vasorelaxation by enhancing 4-aminopyridine-sensitive Kv currents through S-glutathionylation.Pflugers Archiv : European journal of physiology · 2015Article
- Reduced sialylation impacts ventricular repolarization by modulating specific K+ channel isoforms distinctly.The Journal of biological chemistry · 2015Article
- S-glutathionylation of ion channels: insights into the regulation of channel functions, thiol modification crosstalk, and mechanosensing.Antioxidants & redox signaling · 2014Review
- Identifying potential functional impact of mutations and polymorphisms: linking heart failure, increased risk of arrhythmias and sudden cardiac death.Frontiers in physiology · 2013Review
- Molecular determinants of co- and post-translational N-glycosylation of type I transmembrane peptides.The Biochemical journal · 2013Article
- Functional decorations: post-translational modifications and heart disease delineated by targeted proteomics.Genome medicine · 2013Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration. Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo. As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes. Our results show that KCNE1 is exclusively O-glycosylated at Thr-7, which is also required for N-glycosylation at Asn-5. For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein. The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex. The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
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