Evidence map›Paper›PMID 11004206›Full record

ArticleThe Journal of general physiology2000

Ion interactions in the high-affinity binding locus of a voltage-gated Ca(2+) channel.

R K Cloues, S M Cibulsky, W A Sather

Abstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Deciphering CaProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
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  6. Article
  7. Article
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  11. K channel gating by an affinity-switching selectivity filter.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  12. Molecular pharmacology of high voltage-activated calcium channels.Journal of bioenergetics and biomembranes · 2003
    Review
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

R K ClouesDepartment of Pharmacology and Neuroscience Center, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA.
S M Cibulsky
W A Sather

Funding

STATISTICAL COREP01AG004418 · NIA · UNIVERSITY OF SOUTH FLORIDA · PI SMALL, BRENT JOHN · 1985 to 2010
$11.6M
Structural Basis of Ion Selectivity in Calciumn ChannelsR01NS035245 · NINDS · UNIVERSITY OF COLORADO DENVER · PI SATHER, WILLIAM A · 1996 to 2004
$1.2M
CA++ CHANNEL BETA SUBUNITS IN CA++ CHANNEL MODULATIONF31MH011717 · NIMH · UNIVERSITY OF COLORADO DENVER · PI CIBULSKY, SUSAN M · 1997 to 1999
–
NIA NIH HHS AG04418NIA NIH HHS P01 AG004418NIMH NIH HHS F31 MH011717NIMH NIH HHS MH11717NINDS NIH HHS NS35245NINDS NIH HHS R01 NS035245
6 · The paper itself

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.

Indexed as

AnimalsBarium CompoundsBinding SitesCadmium ChlorideCalcium ChannelsChloridesIon Channel GatingLithium ChlorideMutationReproducibility of ResultsXenopusbarium chlorideBarium CompoundsCadmium ChlorideCalcium ChannelsChloridesLithium Chloride

Identifiers

PMID11004206
PMCPMC2230626

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Read underepoch 390

Registered trials

None linked

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.