ArticleProceedings of the National Academy of Sciences of the United States of America2008
Single mutations convert an outward K+ channel into an inward K+ channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 42 citations in OpenAlex.
- Rice ethylene receptors OsERS1/2 function as CaPlant communications · 2026Article
- Article
- Structural changes in the conversion of an Arabidopsis outward-rectifying KPlant communications · 2024Article
- An LQT2-related mutation in the voltage-sensing domain is involved in switching the gating polarity of hERG.BMC biology · 2024Article
- Roles of plastid-located phosphate transporters in carotenoid accumulation.Frontiers in plant science · 2022Review
- Recent Advances in Genome-wide Analyses of Plant Potassium Transporter Families.Current genomics · 2021Review
- Charged pore-lining residues are required for normal channel kinetics in the eukaryotic mechanosensitive ion channel MSL1.Channels (Austin, Tex.) · 2020Article
- Evolution and Structural Characteristics of Plant Voltage-Gated KThe Plant cell · 2018Review
- Functional identification of a GORK potassium channel from the ancient desert shrub Ammopiptanthus mongolicus (Maxim.) Cheng f.Plant cell reports · 2016Article
- Large-scale mutational analysis of Kv11.1 reveals molecular insights into type 2 long QT syndrome.Nature communications · 2014Article
- Involvement of the S4-S5 linker and the C-linker domain regions to voltage-gating in plant Shaker channels: comparison with animal HCN and Kv channels.Plant signaling & behavior · 2014Review
- Cytoplasmic domains and voltage-dependent potassium channel gating.Frontiers in pharmacology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shaker-type K(+) channels in plants display distinct voltage-sensing properties despite sharing sequence and structural similarity. For example, an Arabidopsis K(+) channel (SKOR) and a tomato K(+) channel (LKT1) share high amino acid sequence similarity and identical domain structures; however, SKOR conducts outward K(+) current and is activated by positive membrane potentials (depolarization), whereas LKT1 conducts inward current and is activated by negative membrane potentials (hyperpolarization). The structural basis for the "opposite" voltage-sensing properties of SKOR and LKT1 remains unknown. Using a screening procedure combined with random mutagenesis, we identified in the SKOR channel single amino acid mutations that converted an outward-conducting channel into an inward-conducting channel. Further domain-swapping and random mutagenesis produced similar results, suggesting functional interactions between several regions of SKOR protein that lead to specific voltage-sensing properties. Dramatic changes in rectifying properties can be caused by single amino acid mutations, providing evidence that the inward and outward channels in the Shaker family from plants may derive from the same ancestor.
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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.