Evidence map›Paper›PMID 15201331›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2004

Ligand-dependent activation of Slo family channels is defined by interchangeable cytosolic domains.

Xiao-Ming Xia, Xue Zhang, Christopher J Lingle

Abstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. SLO3 in the fast lane: The latest male contraceptive target with a promising small-molecule inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. A genetic variant of the sperm-specific SLO3 KThe Journal of biological chemistry · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Functional and structural analysis of the human SLO3 pH- and voltage-gated K+ channel.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  18. Review
  19. Structure and function of multiple Ca2+-binding sites in a K+ channel regulator of K+ conductance (RCK) domain.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  20. Review
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.

Xiao-Ming XiaDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Xue Zhang
Christopher J Lingle

Funding

Ion Channel Regulation by Ca2+R01GM066215 · NIGMS · WASHINGTON UNIVERSITY · PI LINGLE, CHRISTOPHER J · 2003 to 2015
$3.6M
NIGMS NIH HHS GM066215NIGMS NIH HHS R01 GM066215
6 · The paper itself

Abstract

Large-conductance Ca2+- and voltage-regulated K+ channels (Slo1 BK-type) are controlled by two physiological stimuli, membrane voltage and cytosolic Ca2+. Regulation by voltage is similar to that in voltage-dependent K+ channels, arising from positively charged amino acids primarily within the S4 transmembrane helices. The basis for regulation by Ca2+ remains controversial. One viewpoint suggests that the extensive cytosolic C terminus contains the Ca2+ regulatory machinery, whereas another suggests that the pore-forming module contains the Ca2+-sensing elements. To address this issue, we take advantage of another Slo family member, the pH-regulated homolog Slo3. We reason that if the ligand-sensing apparatus is uniquely associated with a particular domain (either the pore or the cytosolic domain), exchange of those domains between Slo1 and Slo3 should result in exchange of ligand dependence in association with the key domain. The results show that the Slo3 cytosolic module confers pH-dependent regulation on the Slo1 pore module, whereas the Slo1 cytosolic module confers Ca2+-dependent regulation on the Slo3 pore module. Thus, ligand-specific regulation is defined by interchangeable cytosolic regulatory modules.

Indexed as

AnimalsCalciumCytosolHydrogen-Ion ConcentrationIon Channel GatingLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsMiceOocytesPatch-Clamp TechniquesPotassium Channels, Calcium-ActivatedProtein Structure, TertiaryXenopusCalciumKcnma1 protein, mouseKcnu1 protein, mouseLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsPotassium Channels, Calcium-Activated

Identifiers

PMID15201331
PMCPMC6729329

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.