Evidence map›Paper›PMID 15901836›Full record

ArticleMolecular biology of the cell2005

Structural requirements for differential sensitivity of KCNQ K+ channels to modulation by Ca2+/calmodulin.

Nikita Gamper, Yang Li, Mark S Shapiro

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed, 1 pooled it
4.2field-weighted citation impact, top 5% 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

76 citing papers in PubMed, 1 synthesis or guideline pooled it, 134 citations in OpenAlex.

  1. Calcium and arrhythmogenesis.Physiological reviews · 2007
    Pooled it
  2. Review
  3. Involvement of CaCellular and molecular neurobiology · 2023
    Article
  4. Clinically RelevantInternational journal of molecular sciences · 2022
    Article
  5. Review
  6. Chemical modulation of Kv7 potassium channels.RSC medicinal chemistry · 2021
    Review
  7. Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Atomistic Insights of Calmodulin Gating of Complete Ion Channels.International journal of molecular sciences · 2020
    Review
  12. Genetic intolerance analysis as a tool for protein science.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. A mutually induced conformational fit underlies CaThe Journal of biological chemistry · 2019
    Article
  17. Phosphatidylinositol 4,5-bisphosphate (PIPThe Journal of biological chemistry · 2018
    Article
  18. Article
  19. Review
  20. Article

16 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

3 authors at 1 institution in 1 country.

Nikita GamperDepartment of Physiology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
Yang Li
Mark S Shapiro
The University of Texas Health Science Center at San Antonio · US

Funding

Modulation of Neuronal Ion Channels by 2nd MessengersR01NS043394 · NINDS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI SHAPIRO, MARK S · 2002 to 2014
$4.5M
NINDS NIH HHS NS43394NINDS NIH HHS R01 NS043394
6 · The paper itself

Abstract

Calmodulin modulation of ion channels has emerged as a prominent theme in biology. The sensitivity of KCNQ1-5 K+ channels to modulation by Ca2+/calmodulin (CaM) was studied using patch-clamp, Ca2+ imaging, and biochemical and pharmacological approaches. Coexpression of CaM in Chinese hamster ovary (CHO) cells strongly reduced currents of KCNQ2, KCNQ4, and KCNQ5, but not KCNQ1 or KCNQ3. In simultaneous current recording/Ca2+ imaging experiments, CaM conferred Ca2+ sensitivity to KCNQ4 and KCNQ5, but not to KCNQ1, KCNQ3, or KCNQ1/KCNE1 channels. A chimera constructed from the carboxy terminus of KCNQ4 and the rest KCNQ1 displayed Ca2+ sensitivity similar to KCNQ4. Chimeras constructed from different lengths of the KCNQ4 carboxy terminal and the rest KCNQ3 localized a region that confers sensitivity to Ca2+/CaM. Lobe-specific mutations of CaM revealed that its amino-terminal lobe mediates the Ca2+ sensitivity of the KCNQ/CaM complex. The site of CaM action within the channel carboxy terminus overlaps with that of the KCNQ opener N-ethylmaleimide (NEM). We found that CaM overexpression reduced NEM augmentation of KCNQ2, KCNQ4, and KCNQ5, and NEM pretreatment reduced Ca2+/CaM-mediated suppression of M current in sympathetic neurons by bradykinin. We propose that two functionally distinct types of carboxy termini underlie the observed differences among this channel family.

Indexed as

AnimalsCalciumCalmodulinCells, CulturedCHO CellsCricetinaeElectrophysiologyHumansMalePatch-Clamp TechniquesRatsRecombinant Fusion ProteinsCalciumCalmodulinRecombinant Fusion Proteins

Identifiers

PMID15901836
PMCPMC1182296
OpenAlexW2031749158

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.