ArticlePflugers Archiv : European journal of physiology2012
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.
Article in Pflugers Archiv : European journal of physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026Review
- Calcium Ion Channels inJournal of fungi (Basel, Switzerland) · 2023Review
- Article
- Conformational ensembles of non-peptide ω-conotoxin mimetics and CaComputational and structural biotechnology journal · 2020Article
- Correcting the R165K substitution in the first voltage-sensor of CaChannels (Austin, Tex.) · 2019Article
- New Structures and Gating of Voltage-Dependent Potassium (Kv) Channels and Their Relatives: A Multi-Domain and Dynamic Question.International journal of molecular sciences · 2019Review
- Calcium channel gating.Pflugers Archiv : European journal of physiology · 2018Review
- Correlation between human ether-a-go-go-related gene channel inhibition and action potential prolongation.British journal of pharmacology · 2017Article
- Upward movement of IS4 and IIIS4 is a rate-limiting stage in CaPflugers Archiv : European journal of physiology · 2016Article
- Molecular Interactions in the Voltage Sensor Controlling Gating Properties of CaV Calcium Channels.Structure (London, England : 1993) · 2016Article
- Functional heterogeneity of the four voltage sensors of a human L-type calcium channel.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Methods for quantification of pore-voltage sensor interaction in Ca(V)1.2.Pflugers Archiv : European journal of physiology · 2014Article
- Cooperative activation of the T-type CaV3.2 channel: interaction between Domains II and III.The Journal of biological chemistry · 2013Article
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7 authors.
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Abstract
Voltage sensors trigger the closed-open transitions in the pore of voltage-gated ion channels. To probe the transmission of voltage sensor signalling to the channel pore of Ca(V)1.2, we investigated how elimination of positive charges in the S4 segments (charged residues were replaced by neutral glutamine) modulates gating perturbations induced by mutations in pore-lining S6 segments. Neutralisation of all positively charged residues in IIS4 produced a functional channel (IIS4(N)), while replacement of the charged residues in IS4, IIIS4 and IVS4 segments resulted in nonfunctional channels. The IIS4(N) channel displayed activation kinetics similar to wild type. Mutations in a highly conserved structure motif on S6 segments ("GAGA ring": G432W in IS6, A780T in IIS6, G1193T in IIIS6 and A1503G in IVS6) induce strong left-shifted activation curves and decelerated channel deactivation kinetics. When IIS4(N) was combined with these mutations, the activation curves were shifted back towards wild type and current kinetics were accelerated. In contrast, 12 other mutations adjacent to the GAGA ring in IS6-IVS6, which also affect activation gating, were not rescued by IIS4(N). Thus, the rescue of gating distortions in segments IS6-IVS6 by IIS4(N) is highly position-specific. Thermodynamic cycle analysis supports the hypothesis that IIS4 is energetically coupled with the distantly located GAGA residues. We speculate that conformational changes caused by neutralisation of IIS4 are not restricted to domain II (IIS6) but are transmitted to gating structures in domains I, III and IV via the GAGA ring.
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