ArticleThe Journal of general physiology2005
Functional architecture of the inner pore 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 25 papers.
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Who cites it
25 citing papers in PubMed, 44 citations in OpenAlex.
- CaChannels (Austin, Tex.) · 2020Review
- Congruent pattern of accessibility identifies minimal pore gate in a non-symmetric voltage-gated sodium channel.Nature communications · 2016Article
- Store-Operated Calcium Channels.Physiological reviews · 2015Review
- State-dependent inter-repeat contacts of exceptionally conserved asparagines in the inner helices of sodium and calcium channels.Pflugers Archiv : European journal of physiology · 2015Article
- Ion channel engineering: perspectives and strategies.Journal of molecular biology · 2015Review
- 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
- Neutralisation of a single voltage sensor affects gating determinants in all four pore-forming S6 segments of Ca(V)1.2: a cooperative gating model.Pflugers Archiv : European journal of physiology · 2012Article
- Permeation, selectivity and gating in store-operated CRAC channels.The Journal of physiology · 2012Review
- Domain III regulates N-type (CaV2.2) calcium channel closing kinetics.Journal of neurophysiology · 2012Article
- Identification of new batrachotoxin-sensing residues in segment IIIS6 of the sodium channel.The Journal of biological chemistry · 2011Article
- Physicochemical properties of pore residues predict activation gating of Ca V1.2: a correlation mutation analysis.Pflugers Archiv : European journal of physiology · 2011Article
- The ß subunit of voltage-gated Ca2+ channels.Physiological reviews · 2010Review
- Multi-scale electrophysiology modeling: from atom to organ.The Journal of general physiology · 2010Article
- A homology model of the pore domain of a voltage-gated calcium channel is consistent with available SCAM data.The Journal of general physiology · 2010Article
- Structural model for dihydropyridine binding to L-type calcium channels.The Journal of biological chemistry · 2009Article
- Regulation of voltage-gated Ca2+ channels by lipids.Cell calcium · 2009Review
- Coupled and independent contributions of residues in IS6 and IIS6 to activation gating of CaV1.2.The Journal of biological chemistry · 2009Article
- Bimane fluorescence scanning suggests secondary structure near the S3-S4 linker of BK channels.The Journal of biological chemistry · 2009Article
- 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
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The inner pore of voltage-gated Ca2+ channels (VGCCs) is functionally important, but little is known about the architecture of this region. In K+ channels, this part of the pore is formed by the S6/M2 transmembrane segments from four symmetrically arranged subunits. The Ca2+ channel pore, however, is formed by four asymmetric domains of the same (alpha1) subunit. Here we investigated the architecture of the inner pore of P/Q-type Ca2+ channels using the substituted-cysteine accessibility method. Many positions in the S6 segments of all four repeats of the alpha1 subunit (Ca(v)2.1) were modified by internal methanethiosulfonate ethyltrimethylammonium (MTSET). However, the pattern of modification does not fit any known sequence alignment with K+ channels. In IIS6, five consecutive positions showed clear modification, suggesting a likely aqueous crevice and a loose packing between S6 and S5 segments, a notion further supported by the observation that some S5 positions were also accessible to internal MTSET. These results indicate that the inner pore of VGCCs is indeed formed by the S6 segments but is different from that of K+ channels. Interestingly some residues in IIIS6 and IVS6 whose mutations in L-type Ca2+ channels affect the binding of dihydropyridines and phenylalkylamines and are thought to face the pore appeared not to react with internal MTSET. Probing with qBBr, a rigid thiol-reactive agent with a dimension of 12 angstroms x 10 angstroms x 6 angstroms suggests that the inner pore can open to >10 angstroms. This work provides an impetus for future studies on ion permeation, gating, and drug binding of VGCCs.
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