ArticleProceedings of the National Academy of Sciences of the United States of America2004
Evolving potassium channels by means of yeast selection reveals structural elements important for selectivity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 44 citations in OpenAlex.
- When Is a Potassium Channel Not a Potassium Channel?Function (Oxford, England) · 2022Article
- Pore-forming transmembrane domains control ion selectivity and selectivity filter conformation in the KirBac1.1 potassium channel.The Journal of general physiology · 2021Article
- Review
- Review
- The endosomal trafficking factors CORVET and ESCRT suppress plasma membrane residence of the renal outer medullary potassium channel (ROMK).The Journal of biological chemistry · 2018Article
- Endoplasmic reticulum-associated degradation of the renal potassium channel, ROMK, leads to type II Bartter syndrome.The Journal of biological chemistry · 2017Article
- Tethered protein display identifies a novel Kir3.2 (GIRK2) regulator from protein scaffold libraries.ACS chemical neuroscience · 2014Article
- Silencing of the tandem pore domain halothane-inhibited K+ channel 2 (THIK2) relies on combined intracellular retention and low intrinsic activity at the plasma membrane.The Journal of biological chemistry · 2013Article
- Using yeast to study potassium channel function and interactions with small molecules.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Vitamin A transport and the transmembrane pore in the cell-surface receptor for plasma retinol binding protein.PloS one · 2013Article
- Architecture of the HCN selectivity filter and control of cation permeation.Scientific reports · 2012Article
- K2P potassium channels, mysterious and paradoxically exciting.Science signaling · 2011Article
- Multiple modalities converge on a common gate to control K2P channel function.The EMBO journal · 2011Article
- Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains.The Journal of biological chemistry · 2010Article
- Article
- Searching for interesting channels: pairing selection and molecular evolution methods to study ion channel structure and function.Molecular bioSystems · 2009Review
- An essential ligand-binding domain in the membrane receptor for retinol-binding protein revealed by large-scale mutagenesis and a human polymorphism.The Journal of biological chemistry · 2008Article
- K+/Na+ selectivity in K channels and valinomycin: over-coordination versus cavity-size constraints.Journal of molecular biology · 2008Article
- Non-equivalent role of TM2 gating hinges in heteromeric Kir4.1/Kir5.1 potassium channels.European biophysics journal : EBJ · 2008Article
- Identification of yeast proteins necessary for cell-surface function of a potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Potassium channels are widely distributed. To serve their physiological functions, such as neuronal signaling, control of insulin release, and regulation of heart rate and blood flow, it is essential that K+ channels allow K+ but not the smaller and more abundant Na+ ions to go through. The narrowest part of the channel pore, the selectivity filter formed by backbone carbonyls of the GYG-containing K+ channel signature sequence, approximates the hydration shell of K+ ions. However, the K+ channel signature sequence is not sufficient for K+ selectivity. To identify structural elements important for K+ selectivity, we randomly mutagenized the G protein-coupled inwardly rectifying potassium channel 3.2 (GIRK2) bearing the S177W mutation on the second transmembrane segment. This mutation confers constitutive channel activity but abolishes K+ selectivity and hence the channel's ability to complement the K+ transport deficiency of Deltatrk1Deltatrk2 mutant yeast. S177W-containing GIRK2 mutants that support yeast growth in low-K+ medium contain multiple suppressors, each partially restoring K+ selectivity to S177W-containing double mutants. These suppressors include mutations in the first transmembrane segment and the pore helix, likely exerting long-range actions to restore K+ selectivity, as well as a mutation of a second transmembrane segment residue facing the cytoplasmic half of the pore, below the selectivity filter. Some of these suppressors also affected channel gating (channel open time and opening frequency determined in single-channel analyses), revealing intriguing interplay between ion permeation and channel gating.
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