ArticleThe Journal of biological chemistry2012
Functional analysis of missense mutations in Kv8.2 causing cone dystrophy with supernormal rod electroretinogram.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- A versatile functional interaction between electrically silent KCellular and molecular life sciences : CMLS · 2024Article
- Oxidative Stress Implication in Retinal Diseases-A Review.Antioxidants (Basel, Switzerland) · 2022Review
- Retinoschisin and novel Na/K-ATPase interaction partners Kv2.1 and Kv8.2 define a growing protein complex at the inner segments of mammalian photoreceptors.Cellular and molecular life sciences : CMLS · 2022Article
- Differential impact of Kv8.2 loss on rod and cone signaling and degeneration.Human molecular genetics · 2022Article
- Compound heterozygous KCNV2 variants contribute to cone dystrophy with supernormal rod responses in a Chinese family.Molecular genetics & genomic medicine · 2021Article
- The role of voltage-gated ion channels in visual function and disease in mammalian photoreceptors.Pflugers Archiv : European journal of physiology · 2021Review
- Molecular, Cellular and Functional Changes in the Retinas of Young Adult Mice Lacking the Voltage-Gated KInternational journal of molecular sciences · 2021Article
- Review
- Heteromeric KThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Formation of Functional Heterodimers by TREK-1 and TREK-2 Two-pore Domain Potassium Channel Subunits.The Journal of biological chemistry · 2016Article
- Kv5, Kv6, Kv8, and Kv9 subunits: No simple silent bystanders.The Journal of general physiology · 2016Review
- Novel compound heterozygous mutations resulting in cone dystrophy with supernormal rod response.JAMA ophthalmology · 2013Article
- Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Mutations in KCNV2 have been proposed as the molecular basis for cone dystrophy with supernormal rod electroretinogram. KCNV2 codes for the modulatory voltage-gated potassium channel α-subunit, Kv8.2, which is incapable of forming functional channels on its own. Functional heteromeric channels are however formed with Kv2.1 in heterologous expression systems, with both α-subunit genes expressed in rod and cone photoreceptors. Of the 30 mutations identified in the KCNV2 gene, we have selected three missense mutations localized in the potassium channel pore and two missense mutations localized in the tetramerization domain for analysis. We characterized the differences between homomeric Kv2.1 and heteromeric Kv2.1/Kv8.2 channels and investigated the influence of the selected mutations on the function of heteromeric channels. We found that two pore mutations (W467G and G478R) led to the formation of nonconducting heteromeric Kv2.1/Kv8.2 channels, whereas the mutations localized in the tetramerization domain prevented heteromer generation and resulted in the formation of homomeric Kv2.1 channels only. Consequently, our study suggests the existence of two distinct molecular mechanisms involved in the disease pathology.
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