Evidence map›Paper›PMID 10516302›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1999

Domains responsible for constitutive and Ca(2+)-dependent interactions between calmodulin and small conductance Ca(2+)-activated potassium channels.

J E Keen, R Khawaled, D L Farrens, T Neelands, A Rivard, C T Bond, A Janowsky, B Fakler, J P Adelman, J Maylie

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
5.2field-weighted citation impact, top 4% of its field
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

107 citing papers in PubMed, 219 citations in OpenAlex.

  1. Calmodulin assists during co-translational folding of the KProtein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Redox Regulation of KAntioxidants & redox signaling · 2024
    Review
  6. Review
  7. Calmodulin Mutations in Human Disease.Channels (Austin, Tex.) · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. CaCell calcium · 2022
    Article
  13. NaStructure (London, England : 1993) · 2021
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. The role of calmodulin in regulating calcium-permeable PKD2L1 channel activity.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2019
    Article

47 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 2 countries.

J E KeenVollum Institute, Veteran's Administration Medical Center, and Department of Psychiatry, Behavioral Neuroscience, and Physiology and Pharmacology, Oregon Health Sciences University, Portland Oregon, 97201, USA.
R Khawaled
D L Farrens
T Neelands
A Rivard
C T Bond
A Janowsky
B Fakler
J P Adelman
J Maylie
Vollum Institute · USOregon Health & Science University · USUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small conductance Ca(2+)-activated potassium channels (SK channels) are coassembled complexes of pore-forming SK alpha subunits and calmodulin. We proposed a model for channel activation in which Ca2+ binding to calmodulin induces conformational rearrangements in calmodulin and the alpha subunits that result in channel gating. We now report fluorescence measurements that indicate conformational changes in the alpha subunit after calmodulin binding and Ca2+ binding to the alpha subunit-calmodulin complex. Two-hybrid experiments showed that the Ca(2+)-independent interaction of calmodulin with the alpha subunits requires only the C-terminal domain of calmodulin and is mediated by two noncontiguous subregions; the ability of the E-F hands to bind Ca2+ is not required. Although SK alpha subunits lack a consensus calmodulin-binding motif, mutagenesis experiments identified two positively charged residues required for Ca(2+)-independent interactions with calmodulin. Electrophysiological recordings of SK2 channels in membrane patches from oocytes coexpressing mutant calmodulins revealed that channel gating is mediated by Ca2+ binding to the first and second E-F hand motifs in the N-terminal domain of calmodulin. Taken together, the results support a calmodulin- and Ca(2+)-calmodulin-dependent conformational change in the channel alpha subunits, in which different domains of calmodulin are responsible for Ca(2+)-dependent and Ca(2+)-independent interactions. In addition, calmodulin is associated with each alpha subunit and must bind at least one Ca2+ ion for channel gating. Based on these results, a state model for Ca2+ gating was developed that simulates alterations in SK channel Ca2+ sensitivity and cooperativity associated with mutations in CaM.

Indexed as

Potassium Channels, Calcium-ActivatedAnimalsCalciumCalmodulinFemaleIon Channel GatingModels, BiologicalOocytesPotassium ChannelsRatsSmall-Conductance Calcium-Activated Potassium ChannelsXenopusCalciumCalmodulinKcnn2 protein, ratPotassium ChannelsPotassium Channels, Calcium-ActivatedSmall-Conductance Calcium-Activated Potassium Channels

Identifiers

PMID10516302
PMCPMC6782752
OpenAlexW2118906494

What OpenQuestion holds

Textmetadata
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.