ArticleThe Journal of biological chemistry2010
Functional analysis of the Kv1.1 N255D mutation associated with autosomal dominant hypomagnesemia.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 45 citations in OpenAlex.
- Novel Genetic Variants Expand the Functional, Molecular, and Pathological Diversity ofInternational journal of molecular sciences · 2023Review
- Hereditary kidney diseases associated with hypomagnesemia.Kidney research and clinical practice · 2021Article
- Mechanisms coupling sodium and magnesium reabsorption in the distal convoluted tubule of the kidney.Acta physiologica (Oxford, England) · 2021Review
- Transcriptomic Analysis of Human Mesenchymal Stem Cell Therapy in Incontinent Rat Injured Urethra.Tissue engineering. Part A · 2020Article
- Isoform-Selective KCNA1 Potassium Channel Openers Built from Glycine.The Journal of pharmacology and experimental therapeutics · 2020Article
- Clinical Spectrum ofInternational journal of molecular sciences · 2020Review
- Neuromuscular tetanic hyperexcitability syndrome associated to a heterozygousActa myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2020Article
- iTRAQ-Based Proteomic Analysis of Dentate Gyrus in Temporal Lobe Epilepsy With Hippocampal Sclerosis.Frontiers in neurology · 2020Article
- Silencing of KCNA1 suppresses the cervical cancer development via mitochondria damage.Channels (Austin, Tex.) · 2019Article
- A Kinetic Map of the Homomeric Voltage-Gated Potassium Channel (Kv) Family.Frontiers in cellular neuroscience · 2019Article
- Article
- Role of renal TRP channels in physiology and pathology.Seminars in immunopathology · 2016Review
- Clinical heterogeneity associated with KCNA1 mutations include cataplexy and nonataxic presentations.Neurogenetics · 2016Article
- Distal convoluted tubule.Comprehensive Physiology · 2015Review
- Distal convoluted tubule.Clinical journal of the American Society of Nephrology : CJASN · 2014Review
- Physiological and pathological functions of mechanosensitive ion channels.Molecular neurobiology · 2014Review
- PDB_REDO: constructive validation, more than just looking for errors.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Regulation of magnesium balance: lessons learned from human genetic disease.Clinical kidney journal · 2012Article
- The salt-wasting phenotype of EAST syndrome, a disease with multifaceted symptoms linked to the KCNJ10 K+ channel.Pflugers Archiv : European journal of physiology · 2011Review
- Protein structure analysis of mutations causing inheritable diseases. An e-Science approach with life scientist friendly interfaces.BMC bioinformatics · 2010Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations in the voltage-gated K(+) channel Kv1.1 have been linked with a mixed phenotype of episodic ataxia and/or myokymia. Recently, we presented autosomal dominant hypomagnesemia as a new phenotypic characteristic associated with a mutation in Kv1.1 (N255D) (Glaudemans, B., van der Wijst, J., Scola, R. H., Lorenzoni, P. J., Heister, A., van der Kemp, A. W., Knoers, N. V., Hoenderop, J. G., and Bindels, R. J. (2009) J. Clin. Invest. 119, 936-942). A conserved asparagine at position 255 in the third transmembrane segment was converted into an aspartic acid, resulting in a non-functional channel. In this study, we explored the functional consequence of this conserved residue by substitution with other hydrophobic, polar, or charged amino acids (N255E, N255Q, N255A, N255V, N255T, and N255H). Upon overexpression in human embryonic kidney (HEK293) cells, cell surface biotinylation revealed plasma membrane expression of all mutant channels. Next, we used the whole-cell patch clamp technique to demonstrate that the N255E and N255Q mutants were non-functional. Substitution of Asn-255 with other amino acids (N255A, N255V, N255T, and N255H) did not prevent ion conduction, and these mutant channels activated at more negative potentials when compared with wild-type channels, -41.5 +/- 1.6, -45.5 +/- 2.0, -50.5 +/- 1.9, and -33.8 +/- 1.3 mV to -29.4 +/- 1.1 mV, respectively. The time constant of activation was significantly faster for the two most hydrophobic mutations, N255A (6.2 +/- 0.2 ms) and N255V (5.2 +/- 0.3 ms), and the hydrophilic mutant N255T (9.8 +/- 0.4 ms) in comparison with wild type (13.0 +/- 0.9 ms). Furthermore, the voltage dependence of inactivation was shifted approximately 13 mV to more negative potentials in all mutant channels except for N255H. Taken together, our data showed that an asparagine at position 255 in Kv1.1 is required for normal voltage dependence and kinetics of channel gating.
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