Evidence map›Paper›PMID 18339689›Full record

ArticleThe Journal of physiology2008

Calmodulin binding to M-type K+ channels assayed by TIRF/FRET in living cells.

Manjot Bal, Oleg Zaika, Pamela Martin, Mark S Shapiro

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Local CaScience signaling · 2020
    Article
  6. Article
  7. Combining TIR and FRET in Molecular Test Systems.International journal of molecular sciences · 2019
    Article
  8. Single-Molecule FRET Methods to Study Glutamate Receptors.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  9. Review
  10. Structural basis and energy landscape for the CaProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Regulation of neuronal M-channel gating in an isoform-specific manner: functional interplay between calmodulin and syntaxin 1A.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    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

4 authors at 1 institution in 1 country.

Manjot BalUniversity of Texas Health Science Center at San Antonio, Department of Physiology, MS 7756, San Antonio, TX 78229, USA.
Oleg Zaika
Pamela Martin
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 R01 NS043394
6 · The paper itself

Abstract

Calmodulin (CaM) binds to KCNQ2-4 channels within their carboxy termini, where it regulates channel function. The existing data have not resolved the Ca2+ dependence of the interaction between the channels and CaM. We performed glutathione S-transferase (GST)-pull-down assays between purified KCNQ2-4 carboxy termini and CaM proteins to determine the Ca2+ dependence of the interaction in vitro. The assays showed substantial Ca2+ dependence of the interaction of the channels with wild-type (WT) CaM, but not with dominant-negative (DN) CaM. To demonstrate CaM-channel interactions in individual living cells, we performed fluorescence resonance energy transfer (FRET) between ECFP-tagged KCNQ2-4 channels and EYFP-tagged CaM expressed in CHO cells, performed under total internal reflection fluorescence (TIRF) microscopy, in which excitation light only penetrates several hundred nanometres into the cell, thus isolating membrane events. FRET was assayed between the channels and either WT or DN CaM, performed under conditions of normal [Ca2+]i, low [Ca2+]i or high [Ca2+]i induced by empirically optimized bathing solutions. The FRET data suggest a strong Ca2+ dependence for the interaction between WT CaM and KCNQ2, but less so for KCNQ3 and KCNQ4. FRET between all KCNQ2-4 channels and DN CaM was robust, and not significantly Ca2+ dependent. These data show interactions between CaM and KCNQ channels in living cells, and suggest that the interactions between KCNQ2-4 channels and CaM are likely to have Ca2+-dependent and Ca2+-independent components.

Indexed as

AnimalsCalciumCalmodulinCHO CellsCricetinaeCricetulusFluorescence Resonance Energy TransferIon Channel GatingKCNQ Potassium ChannelsMicroscopy, FluorescenceProtein BindingProtein Interaction MappingSignal TransductionCalciumCalmodulinKCNQ Potassium Channels

Identifiers

PMID18339689
PMCPMC2479561
OpenAlexW1654307180

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.