ArticleThe Journal of general physiology2001
Permeant ion-dependent changes in gating of Kir2.1 inward rectifier potassium channels.
Article in The Journal of general physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Similarity of the ion occupations of KChannels (Austin, Tex.) · 2026Article
- Permeant cations modulate pore dynamics and gating of TRPV1 ion channels.The Journal of general physiology · 2024Article
- Site-specific ion occupation in the selectivity filter causes voltage-dependent gating in a viral KScientific reports · 2018Article
- Extended beta distributions open the access to fast gating in bilayer experiments-assigning the voltage-dependent gating to the selectivity filter.FEBS letters · 2017Article
- Control of Kir channel gating by cytoplasmic domain interface interactions.The Journal of general physiology · 2017Article
- The pore structure and gating mechanism of K2P channels.The EMBO journal · 2011Article
- On the structural basis of modal gating behavior in K(+) channels.Nature structural & molecular biology · 2011Article
- An NAADP-gated two-pore channel targeted to the plasma membrane uncouples triggering from amplifying Ca2+ signals.The Journal of biological chemistry · 2010Article
- KirBac1.1: it's an inward rectifying potassium channel.The Journal of general physiology · 2009Article
- Phosphatidylinositol-4,5-bisphosphate (PIP2) regulation of strong inward rectifier Kir2.1 channels: multilevel positive cooperativity.The Journal of physiology · 2008Article
- Tl+-induced micros gating of current indicates instability of the MaxiK selectivity filter as caused by ion/pore interaction.The Journal of general physiology · 2008Article
- Saturation and microsecond gating of current indicate depletion-induced instability of the MaxiK selectivity filter.The Journal of general physiology · 2007Article
- Relationship between pore occupancy and gating in BK potassium channels.The Journal of general physiology · 2006Article
- Functional roles of charged amino acid residues on the wall of the cytoplasmic pore of Kir2.1.The Journal of general physiology · 2006Article
- Filter flexibility and distortion in a bacterial inward rectifier K+ channel: simulation studies of KirBac1.1.Biophysical journal · 2004Article
- Influence of permeant ions on voltage sensor function in the Kv2.1 potassium channel.The Journal of general physiology · 2004Article
- Evolving potassium channels by means of yeast selection reveals structural elements important for selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Gating mechanism of KATP channels: function fits form.The Journal of general physiology · 2003Review
- The pore helix is involved in stabilizing the open state of inwardly rectifying K+ channels.Biophysical journal · 2003Article
- Isoprenaline-stimulated differential adrenergic response of K+ channels in skeletal muscle under hypokalaemic conditions.Pflugers Archiv : European journal of physiology · 2003Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We studied the effect of monovalent thallium ion (Tl(+)) on the gating of single Kir2.1 channels, which open and close spontaneously at a constant membrane potential. In cell-attached recordings of single-channel inward current, changing the external permeant ion from K(+) to Tl(+) decreases the mean open-time by approximately 20-fold. Furthermore, the channel resides predominantly at a subconductance level, which results from a slow decay (tau = 2.7 ms at -100 mV) from the fully open level immediately following channel opening. Mutation of a pore-lining cysteine (C169) to valine abolishes the slow decay and subconductance level, and single-channel recordings from channels formed by tandem tetramers containing one to three C169V mutant subunits indicate that Tl(+) must interact with at least three C169 residues to induce these effects. However, the C169V mutation does not alter the single-channel closing kinetics of Tl(+) current. These results suggest that Tl(+) ions change the conformation of the ion conduction pathway during permeation and alter gating by two distinct mechanisms. First, they interact with the thiolate groups of C169 lining the cavity to induce conformational changes of the ion passageway, and thereby produce a slow decay of single-channel current and a dominant subconductance state. Second, they interact more strongly than K(+) with the main chain carbonyl oxygens lining the selectivity filter to destabilize the open state of the channel and, thus, alter the open/close kinetics of gating. In addition to altering gating, Tl(+) greatly diminishes Ba(2+) block. The unblocking rate of Ba(2+) is increased by >22-fold when the external permeant ion is switched from K(+) to Tl(+) regardless of the direction of Ba(2+) exit. This effect cannot be explained solely by ion-ion interactions, but is consistent with the notion that Tl(+) induces conformational changes in the selectivity filter.
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