ArticlePflugers Archiv : European journal of physiology2006
Evidence for common structural determinants of activation and inactivation in T-type Ca2+ channels.
Article in Pflugers Archiv : European journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- The four voltage-sensing domains of T-type calcium channels activate near the resting membrane potential.Nature communications · 2026Article
- CaChannels (Austin, Tex.) · 2020Review
- Upward movement of IS4 and IIIS4 is a rate-limiting stage in CaPflugers Archiv : European journal of physiology · 2016Article
- Contrasting the roles of the I-II loop gating brake in CaV3.1 and CaV3.3 calcium channels.Pflugers Archiv : European journal of physiology · 2015Article
- Ins and outs of T-channel structure function.Pflugers Archiv : European journal of physiology · 2014Review
- Amazing T-type calcium channels: updating functional properties in health and disease.Pflugers Archiv : European journal of physiology · 2014Review
- 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
- 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
- Calcium currents of olfactory bulb juxtaglomerular cells: profile and multiple conductance plateau potential simulation.Neuroscience · 2011Article
- The voltage dependence of gating currents of the neuronal CA(v)3.3 channel is determined by the gating brake in the I-II loop.Pflugers Archiv : European journal of physiology · 2011Article
- Cysteines in the loop between IS5 and the pore helix of Ca(V)3.1 are essential for channel gating.Pflugers Archiv : European journal of physiology · 2010Article
- Transient and big are key features of an invertebrate T-type channel (LCav3) from the central nervous system of Lymnaea stagnalis.The Journal of biological chemistry · 2010Article
- I-II loop structural determinants in the gating and surface expression of low voltage-activated calcium channels.PloS one · 2008Article
- Permeation and gating in CaV3.1 (alpha1G) T-type calcium channels effects of Ca2+, Ba2+, Mg2+, and Na+.The Journal of general physiology · 2008Article
- Characterization of the gating brake in the I-II loop of Ca(v)3.2 T-type Ca(2+) channels.The Journal of biological chemistry · 2008Article
- Subunit-specific modulation of T-type calcium channels by zinc.The Journal of physiology · 2007Article
- Pore stability and gating in voltage-activated calcium channels.Channels (Austin, Tex.)Review
- Characterization of the gating brake in the I-II loop of CaV3 T-type calcium channels.Channels (Austin, Tex.)Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the most distinctive features of T-type Ca(2+) channels is their fast inactivation. Recent structure-function studies indicate that the rate of macroscopic inactivation of these channels is influenced by several structural components, including intracellular linkers, transmembrane segments, and pore loops. The macroscopic inactivation of T-type channels is partially coupled to activation. It is therefore possible that changes in the rate of macroscopic inactivation after alteration in the structure of these channels might actually result from changes in activation kinetics. In this study, we use kinetic simulations to illustrate how the alteration of the rate of channel activation may lead to changes in the rate of macroscopic inactivation. By examining data pooled from several structure-function studies we demonstrate that gating modifications induced by alteration in the channel structure unveils a correlation between the time constants of macroscopic inactivation and activation. This analysis underscores the relevance of considering the inactivation-activation coupling when analyzing the structural determinants of T-type channel inactivation. Furthermore, we demonstrate that slow-inactivating mutants, with modifications in the IIIS6 segment and the proximal C terminus, display significant alterations in the voltage dependencies of activation and deactivation with respect to the wild type channel Ca(V)3.1. Our results indicate that common structures, most likely the S6 transmembrane segments, are involved in the conformational changes occurring during both channel activation and inactivation.
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