ArticleThe Journal of general physiology2000
Ion interactions in the high-affinity binding locus of a voltage-gated Ca(2+) channel.
Article in The Journal of general physiology, 2000. 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.
- Deciphering CaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- CaV1.2 channelopathic mutations evoke diverse pathophysiological mechanisms.The Journal of general physiology · 2022Article
- Physiological Alterations of Subchronic Lead Exposure Induced Degeneration of Epithelial Cells in Proximal Tubules and the Remedial Effect of Curcumin-III in Meriones shawi: a Possible Link with Vasopressin Release.Biological trace element research · 2022Article
- Article
- Article
- Futile Na+ cycling at the root plasma membrane in rice (Oryza sativa L.): kinetics, energetics, and relationship to salinity tolerance.Journal of experimental botany · 2008Article
- Molecular determinant for specific Ca/Ba selectivity profiles of low and high threshold Ca2+ channels.The Journal of general physiology · 2007Article
- Block of CaV1.2 channels by Gd3+ reveals preopening transitions in the selectivity filter.The Journal of general physiology · 2007Article
- G protein {beta}{gamma} subunits mediate presynaptic inhibition of transmitter release from rat superior cervical ganglion neurones in culture.The Journal of physiology · 2005Article
- Y3+ block demonstrates an intracellular activation gate for the alpha1G T-type Ca2+ channel.The Journal of general physiology · 2004Article
- K channel gating by an affinity-switching selectivity filter.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Molecular pharmacology of high voltage-activated calcium channels.Journal of bioenergetics and biomembranes · 2003Review
- The cation selectivity filter of the bacterial sodium channel, NaChBac.The Journal of general physiology · 2002Article
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Authors and funding
3 authors.
Funding
Abstract
The selectivity filter of voltage-gated Ca(2+) channels is in part composed of four Glu residues, termed the EEEE locus. Ion selectivity in Ca(2+) channels is based on interactions between permeant ions and the EEEE locus: in a mixture of ions, all of which can pass through the pore when present alone, those ions that bind weakly are impermeant, those that bind more strongly are permeant, and those that bind more strongly yet act as pore blockers as a consequence of their low rate of unbinding from the EEEE locus. Thus, competition among ion species is a determining feature of selectivity filter function in Ca(2+) channels. Previous work has shown that Asp and Ala substitutions in the EEEE locus reduce ion selectivity by weakening ion binding affinity. Here we describe for wild-type and EEEE locus mutants an analysis at the single channel level of competition between Cd(2+), which binds very tightly within the EEEE locus, and Ba(2+) or Li(+), which bind less tightly and hence exhibit high flux rates: Cd(2+) binds to the EEEE locus approximately 10(4)x more tightly than does Ba(2+), and approximately 10(8)x more tightly than does Li(+). For wild-type channels, Cd(2+) entry into the EEEE locus was 400x faster when Li(+) rather than Ba(2+) was the current carrier, reflecting the large difference between Ba(2+) and Li(+) in affinity for the EEEE locus. For the substitution mutants, analysis of Cd(2+) block kinetics shows that their weakened ion binding affinity can result from either a reduction in blocker on rate or an enhancement of blocker off rate. Which of these rate effects underlay weakened binding was not specified by the nature of the mutation (Asp vs. Ala), but was instead determined by the valence and affinity of the current-carrying ion (Ba(2+) vs. Li(+)). The dependence of Cd(2+) block kinetics upon properties of the current-carrying ion can be understood by considering the number of EEEE locus oxygen atoms available to interact with the different ion pairs.
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