ArticleThe Journal of physiology2001
Control of rectification and permeation by two distinct sites after the second transmembrane region in Kir2.1 K+ channel.
Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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Who cites it
80 citing papers in PubMed.
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
- Repurposing polyamines to prevent life-threatening arrhythmias in Short QT Syndrome type 3.Nature communications · 2026Article
- A Novel KCNJ2 p.Glu299Ala Variant Associated with Short QT Phenotype and Persistent Atrial Fibrillation in a Child.Life (Basel, Switzerland) · 2026Article
- The network of cardiac KNaunyn-Schmiedeberg's archives of pharmacology · 2024Review
- The Kir2.1E299V mutation increases atrial fibrillation vulnerability while protecting the ventricles against arrhythmias in a mouse model of short QT syndrome type 3.Cardiovascular research · 2024Article
- Electro-metabolic signaling.The Journal of general physiology · 2024Article
- Gating and modulation of an inward-rectifier potassium channel.The Journal of general physiology · 2023Article
- Cryo-electron microscopy unveils unique structural features of the human Kir2.1 channel.Science advances · 2022Article
- Cardiac potassium inward rectifier Kir2: Review of structure, regulation, pharmacology, and arrhythmogenesis.Heart rhythm · 2021Review
- Kir4.1/Kir5.1 channels possess strong intrinsic inward rectification determined by a voltage-dependent K+-flux gating mechanism.The Journal of general physiology · 2021Article
- Comparison of KHandbook of experimental pharmacology · 2021Article
- Kir Channel Molecular Physiology, Pharmacology, and Therapeutic Implications.Handbook of experimental pharmacology · 2021Review
- Computational Insights Into Voltage Dependence of Polyamine Block in a Strong Inwardly Rectifying KFrontiers in pharmacology · 2020Article
- Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019Article
- Domain insertion permissibility-guided engineering of allostery in ion channels.Nature communications · 2019Article
- Polyamines and potassium channels: A 25-year romance.The Journal of biological chemistry · 2018Review
- Linkage analysis reveals allosteric coupling in Kir2.1 channels.The Journal of general physiology · 2018Article
- External KThe Journal of general physiology · 2018Article
- Kir2 inward rectification-controlled precise and dynamic balances between Kir2 and HCN currents initiate pacemaking activity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Kir2.1 channels set two levels of resting membrane potential with inward rectification.Pflugers Archiv : European journal of physiology · 2018Article
20 more citing papers are in PubMed but not listed here.
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. The rectification property of the inward rectifier K+ channel is chiefly due to the block of outward current by cytoplasmic Mg2+ and polyamines. In the cloned inward rectifier K+ channel Kir2.1 (IRK1), Asp172 in the second transmembrane region (M2) and Glu224 in the putative cytoplasmic region after M2 are reported to be critical for the sensitivity to these blockers. However, the difference in the inward rectification properties between Kir2.1 and a very weak inward rectifier sWIRK could not be explained by differences at these two sites. 2. Following sequence comparison of Kir2.1 and sWIRK, we focused this study on Glu299 located in the centre of the putative cytoplasmic region after M2. Single-point mutants of Kir2.1 (Glu224Gly and Glu299Ser) and a double-point mutant (Glu224Gly-Glu299Ser) were made and expressed in Xenopus oocytes or in HEK293T cells. 3. Their electrophysiological properties were compared with those of wild-type (WT) Kir2.1 and the following observations were made. (a) Glu299Ser showed a weaker inward rectification, a slower activation upon hyperpolarization, a slower decay of the outward current upon depolarization, a lower sensitivity to block by cytoplasmic spermine and a smaller single-channel conductance than WT. (b) The features of Glu224Gly were similar to those of Glu299Ser. (c) In the double mutant (Glu224Gly-Glu299Ser), the differences from WT described above were more prominent. 4. These results demonstrate that Glu299 as well as Glu224 control rectification and permeation, and suggest the possibility that the two sites contribute to the inner vestibule of the channel pore. The slowing down of the on- and off-blocking processes by mutation of these sites implies that Glu224 and Glu299 function to facilitate the entry (and exit) of spermine to (and from) the blocking site.
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