ArticleThe Journal of general physiology2005
Localization of the activation gate of a voltage-gated Ca2+ channel.
Article in The Journal of general physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
24 citing papers in PubMed, 34 citations in OpenAlex.
- Inactivation of CaV1 and CaV2 channels.The Journal of general physiology · 2025Review
- Calcium Ion Channels inJournal of fungi (Basel, Switzerland) · 2023Review
- De novo variants in CACNA1E found in patients with intellectual disability, developmental regression and social cognition deficit but no seizures.Molecular autism · 2021Article
- Article
- Calcium channel gating.Pflugers Archiv : European journal of physiology · 2018Review
- Conformational plasticity in the selectivity filter of the TRPV2 ion channel.Nature structural & molecular biology · 2018Article
- Congruent pattern of accessibility identifies minimal pore gate in a non-symmetric voltage-gated sodium channel.Nature communications · 2016Article
- Arrhythmogenesis in Timothy Syndrome is associated with defects in Ca(2+)-dependent inactivation.Nature communications · 2016Article
- Calcium ions open a selectivity filter gate during activation of the MthK potassium channel.Nature communications · 2015Article
- Evolutionarily conserved intracellular gate of voltage-dependent sodium channels.Nature communications · 2014Article
- Structure and function of the β subunit of voltage-gated Ca²⁺ channels.Biochimica et biophysica acta · 2013Review
- How "Pharmacoresistant" is Cav2.3, the Major Component of Voltage-Gated R-type Ca2+ Channels?Pharmaceuticals (Basel, Switzerland) · 2013Article
- Dynamic switching of calmodulin interactions underlies Ca2+ regulation of CaV1.3 channels.Nature communications · 2013Article
- Domain III regulates N-type (CaV2.2) calcium channel closing kinetics.Journal of neurophysiology · 2012Article
- The ß subunit of voltage-gated Ca2+ channels.Physiological reviews · 2010Review
- Molecular endpoints of Ca2+/calmodulin- and voltage-dependent inactivation of Ca(v)1.3 channels.The Journal of general physiology · 2010Article
- Regulation of voltage-gated Ca2+ channels by lipids.Cell calcium · 2009Review
- Origin of the voltage dependence of G-protein regulation of P/Q-type Ca2+ channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Introduction into Ca(v)2.1 of the homologous mutation of Ca(v)1.2 causing the Timothy syndrome questions the role of V421 in the phenotypic definition of P-type Ca(2+) channel.Pflugers Archiv : European journal of physiology · 2008Article
- The activation gate and gating mechanism of the NMDA receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Ion channels open and close in response to changes in transmembrane voltage or ligand concentration. Recent studies show that K+ channels possess two gates, one at the intracellular end of the pore and the other at the selectivity filter. In this study we determined the location of the activation gate in a voltage-gated Ca2+ channel (VGCC) by examining the open/closed state dependence of the rate of modification by intracellular methanethiosulfonate ethyltrimethylammonium (MTSET) of pore-lining cysteines engineered in the S6 segments of the alpha1 subunit of P/Q type Ca2+ channels. We found that positions above the putative membrane/cytoplasm interface, including two positions below the corresponding S6 bundle crossing in K+ channels, showed pronounced state-dependent accessibility to internal MTSET, reacting approximately 1,000-fold faster with MTSET in the open state than in the closed state. In contrast, a position at or below the putative membrane/cytoplasm interface was modified equally rapidly in both the open and closed states. Our results suggest that the S6 helices of the alpha1 subunit of VGCCs undergo conformation changes during gating and the activation gate is located at the intracellular end of the pore.
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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.