ArticleThe Journal of general physiology2007
The role of the cytoplasmic pore in inward rectification of Kir2.1 channels.
Article in The Journal of general physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Channel rectification made simple.Biophysical journal · 2025Article
- Cloning, functional expression, and pharmacological characterization of inwardly rectifying potassium channels (Kir) from Apis mellifera.Scientific reports · 2024Article
- Gating and modulation of an inward-rectifier potassium channel.The Journal of general physiology · 2023Article
- Computational Insights Into Voltage Dependence of Polyamine Block in a Strong Inwardly Rectifying KFrontiers in pharmacology · 2020Article
- Polyamines and potassium channels: A 25-year romance.The Journal of biological chemistry · 2018Review
- Inhibition of inwardly rectifying Kir2.x channels by the novel anti-cancer agent gambogic acid depends on both pore block and PIPNaunyn-Schmiedeberg's archives of pharmacology · 2017Article
- Conformational changes at cytoplasmic intersubunit interactions control Kir channel gating.The Journal of biological chemistry · 2017Article
- Novel KCNJ10 Gene Variations Compromise Function of Inwardly Rectifying Potassium Channel 4.1.The Journal of biological chemistry · 2016Article
- The bundle crossing region is responsible for the inwardly rectifying internal spermine block of the Kir2.1 channel.Pflugers Archiv : European journal of physiology · 2014Article
- Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.The Journal of biological chemistry · 2014Article
- Inward rectifiers and their regulation by endogenous polyamines.Frontiers in physiology · 2014Review
- Scanning the topography of polyamine blocker binding in an inwardly rectifying potassium channel.The Journal of biological chemistry · 2013Article
- Multi-ion distributions in the cytoplasmic domain of inward rectifier potassium channels.Biophysical journal · 2012Article
- Locale and chemistry of spermine binding in the archetypal inward rectifier Kir2.1.The Journal of general physiology · 2010Article
- Ionic flow enhances low-affinity binding: a revised mechanistic view into Mg2+ block of NMDA receptors.The Journal of physiology · 2010Article
- Crystal structure of the eukaryotic strong inward-rectifier K+ channel Kir2.2 at 3.1 A resolution.Science (New York, N.Y.) · 2009Article
- A comprehensive guide to the ROMK potassium channel: form and function in health and disease.American journal of physiology. Renal physiology · 2009Review
- Evidence for the direct interaction of spermine with the inwardly rectifying potassium channel.The Journal of biological chemistry · 2009Article
- Mammalian polyamine metabolism and function.IUBMB life · 2009Review
- Long-pore electrostatics in inward-rectifier potassium channels.The Journal of general physiology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Steeply voltage-dependent block by intracellular polyamines underlies the strong inward rectification properties of Kir2.1 and other Kir channels. Mutagenesis studies have identified several negatively charged pore-lining residues (D172, E224, and E299, in Kir2.1) in the inner cavity and cytoplasmic domain as determinants of the properties of spermine block. Recent crystallographic determination of the structure of the cytoplasmic domains of Kir2.1 identified additional negatively charged residues (D255 and D259) that influence inward rectification. In this study, we have characterized the kinetic and steady-state properties of spermine block in WT Kir2.1 and in mutations of the D255 residue (D255E, A, K, R). Despite minimal effects on steady-state blockade by spermine, D255 mutations have profound effects on the blocking kinetics, with D255A marginally, and D255R dramatically, slowing the rate of block. In addition, these mutations result in the appearance of a sustained current (in the presence of spermine) at depolarized voltages. These features are reproduced with a kinetic model consisting of a single open state, two sequentially linked blocked states, and a slow spermine permeation step, with residue D255 influencing the spermine affinity and rate of entry into the shallow blocked state. The data highlight a "long-pore" effect in Kir channels, and emphasize the importance of considering blocker permeation when assessing the effects of mutations on apparent blocker affinity.
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Registered trials
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.