ArticleThe Journal of physiology2004
Inactivation and recovery in Kv1.4 K+ channels: lipophilic interactions at the intracellular mouth of the pore.
Article in The Journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Reverse-engineered models reveal differential membrane properties of autonomic and cutaneous unmyelinated fibers.PLoS computational biology · 2024Article
- Unmasking subtype-dependent susceptibility to C-type inactivation in mammalian Kv1 channels.Biophysical journal · 2024Article
- Shaker-IR K+ channel gating in heavy water: Role of structural water molecules in inactivation.The Journal of general physiology · 2021Article
- Pharmacology of A-Type KHandbook of experimental pharmacology · 2021Article
- Open channel block of Kv1.4 potassium channels by aripiprazole.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2020Article
- The Effects of 4-Hydroxybenzoic Acid Identified from Bamboo (The Malaysian journal of medical sciences : MJMS · 2018Article
- Synaptotagmin I delays the fast inactivation of Kv1.4 channel through interaction with its N-terminus.Molecular brain · 2014Article
- Ginseng ginsenoside pharmacology in the nervous system: involvement in the regulation of ion channels and receptors.Frontiers in physiology · 2014Review
- Interaction of the S6 proline hinge with N-type and C-type inactivation in Kv1.4 channels.Biophysical journal · 2012Article
- Markov models of use-dependence and reverse use-dependence during the mouse cardiac action potential.PloS one · 2012Article
- Postnatal development of A-type and Kv1- and Kv2-mediated potassium channel currents in neocortical pyramidal neurons.Journal of neurophysiology · 2011Article
- A model of the interaction between N-type and C-type inactivation in Kv1.4 channels.Biophysical journal · 2011Article
- A molecular switch between the outer and the inner vestibules of the voltage-gated Na+ channel.The Journal of biological chemistry · 2010Article
- Article
- Modification of K+ channel-drug interactions by ancillary subunits.The Journal of physiology · 2008Review
- Ancillary subunits and stimulation frequency determine the potency of chromanol 293B block of the KCNQ1 potassium channel.The Journal of physiology · 2006Article
- Transient outward potassium current, 'Ito', phenotypes in the mammalian left ventricle: underlying molecular, cellular and biophysical mechanisms.The Journal of physiology · 2005Review
- Shab K (+) channel slow inactivation: a test for U-type inactivation and a hypothesis regarding K (+) -facilitated inactivation mechanisms.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
C-type inactivation is present in many voltage-gated potassium channels and is probably related to 'slow' inactivation in calcium and sodium channels. The mechanisms underlying C-type inactivation are unclear, but it is sensitive to mutations on both the extra- and intracellular sides of the channel. We used an N-terminal deleted channel with a valine to alanine point mutation at the intracellular side of S6 (fKv1.4[V561A]DeltaN). This construct alters recovery from inactivation and inverts the relationship between C-type inactivation and [K(+)](o). We used this inverted relationship to examine C-type inactivation and coupling mechanisms between N- and C-type inactivation. The valine to alanine mutation reduces the channel's affinity for both quinidine and the N-terminal domain. However, binding of the N-terminal or quinidine restores normal recovery from inactivation. This suggests that coupling between N- and C-type inactivation is dominated by allosteric mechanisms. The permeation mechanism, driven by a reduction in permeant [K(+)](o) following pore block (which would retard C-type inactivation), contributes minimally to coupling in these channels. We propose that the cytoplasmic half of S6 forms part of the N-terminal binding site, as previously predicted from X-ray crystallography studies in the distantly related KcsA channel. Binding of the N-terminal domain or a positively charged lipophilic compound such as quinidine interacts with the hydrophobic moieties on S6 in the bound state. This binding can orientate S6 into a conformation which resembles the normal C-type inactivated state. This is the probable mechanism by which drug or N-terminal binding increases the rate of C-type inactivation via an allosteric mechanism.
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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.