Evidence map›Paper›PMID 20385812›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Dual role of protein kinase C on BK channel regulation.

Xiao-Bo Zhou, Iris Wulfsen, Emine Utku, Ulrike Sausbier, Matthias Sausbier, Thomas Wieland, Peter Ruth, Michael Korth

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Protein kinase Cγ in cerebellar Purkinje cells regulates CaProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Review
  8. Coronary Large Conductance CaFrontiers in physiology · 2021
    Review
  9. BKAntioxidants (Basel, Switzerland) · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Large-conductance CaThe Journal of physiology · 2017
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

8 authors at 4 institutions in 1 country.

Xiao-Bo ZhouInstitute of Pharmacology for Pharmacists, University Medical Center Hamburg-Eppendorf, D-20246 Hamburg, Germany.
Iris Wulfsen
Emine Utku
Ulrike Sausbier
Matthias Sausbier
Thomas Wieland
Peter Ruth
Michael Korth
University of Tübingen · DEUniversität Hamburg · DEUniversity Medical Center Hamburg-Eppendorf · DEUniversity Medical Centre Mannheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Large conductance voltage- and Ca(2+)-activated potassium channels (BK channels) are important feedback regulators in excitable cells and are potently regulated by protein kinases. The present study reveals a dual role of protein kinase C (PKC) on BK channel regulation. Phosphorylation of S(695) by PKC, located between the two regulators of K(+) conductance (RCK1/2) domains, inhibits BK channel open-state probability. This PKC-dependent inhibition depends on a preceding phosphorylation of S(1151) in the C terminus of the channel alpha-subunit. Phosphorylation of only one alpha-subunit at S(1151) and S(695) within the tetrameric pore is sufficient to inhibit BK channel activity. We further detected that protein phosphatase 1 is associated with the channel, constantly counteracting phosphorylation of S(695). PKC phosphorylation at S(1151) also influences stimulation of BK channel activity by protein kinase G (PKG) and protein kinase A (PKA). Though the S(1151)A mutant channel is activated by PKA only, the phosphorylation of S(1151) by PKC renders the channel responsive to activation by PKG but prevents activation by PKA. Phosphorylation of S(695) by PKC or introducing a phosphomimetic aspartate at this position (S(695)D) renders BK channels insensitive to the stimulatory effect of PKG or PKA. Therefore, our findings suggest a very dynamic regulation of the channel by the local PKC activity. It is shown that this complex regulation is not only effective in recombinant channels but also in native BK channels from tracheal smooth muscle.

Indexed as

Analysis of VarianceAnimalsCattleCell LineCyclic AMP-Dependent Protein KinasesCyclic GMP-Dependent Protein KinasesElectrophysiologyHumansLarge-Conductance Calcium-Activated Potassium ChannelsMiceMice, Inbred C57BLMutagenesis, Site-DirectedMyocytes, Smooth MusclePatch-Clamp TechniquesPhosphorylationProtein Kinase CCyclic AMP-Dependent Protein KinasesCyclic GMP-Dependent Protein KinasesLarge-Conductance Calcium-Activated Potassium ChannelsProtein Kinase CProtein Phosphatase 1

Identifiers

PMID20385812
PMCPMC2867903
OpenAlexW2048644561

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.