Evidence map›Paper›PMID 15280542›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Distinct stoichiometry of BKCa channel tetramer phosphorylation specifies channel activation and inhibition by cAMP-dependent protein kinase.

Lijun Tian, Lorraine S Coghill, Heather McClafferty, Stephen H-F MacDonald, Ferenc A Antoni, Peter Ruth, Hans-Guenther Knaus, Michael J Shipston

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. 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
2.3field-weighted citation impact, top 12% 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, 104 citations in OpenAlex.

  1. Article
  2. Cytochrome C-like Domain Within the Human BK Channel.International journal of molecular sciences · 2025
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Large-conductance CaThe Journal of physiology · 2017
    Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. MaxiK channel and cell signalling.Pflugers Archiv : European journal of physiology · 2014
    Review
  15. Review
  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 2 institutions in 2 countries.

Lijun TianMembrane Biology Group, Division of Biomedical Science, University of Edinburgh, Edinburgh EH8 9XD, United Kingdom.
Lorraine S Coghill
Heather McClafferty
Stephen H-F MacDonald
Ferenc A Antoni
Peter Ruth
Hans-Guenther Knaus
Michael J Shipston
University of Edinburgh · GBUniversität Innsbruck · AT

Funding

Wellcome Trust 067683
6 · The paper itself

Abstract

Large conductance voltage- and calcium-activated potassium (BK(Ca)) channels are important signaling molecules that are regulated by multiple protein kinases and protein phosphatases at multiple sites. The pore-forming alpha-subunits, derived from a single gene that undergoes extensive alternative pre-mRNA splicing, assemble as tetramers. Although consensus phosphorylation sites have been identified within the C-terminal domain of alpha-subunits, it is not known whether phosphorylation of all or single alpha-subunits within the tetramer is required for functional regulation of the channel. Here, we have exploited a strategy to study single-ion channels in which both the alpha-subunit splice-variant composition is defined and the number of consensus phosphorylation sites available within each tetramer is known. We have used this approach to demonstrate that cAMP-dependent protein kinase (PKA) phosphorylation of the conserved C-terminal PKA consensus site (S899) in all four alpha-subunits is required for channel activation. In contrast, inhibition of BK(Ca) channel activity requires phosphorylation of only a single alpha-subunit at a splice insert (STREX)-specific PKA consensus site (S4(STREX)). Thus, distinct modes of BK(Ca) channel regulation by PKA phosphorylation exist: an "all-or-nothing" rule for activation and a "single-subunit" rule for inhibition. This essentially digital regulation has important implications for the combinatorial and conditional regulation of BK(Ca) channels by reversible protein phosphorylation.

Indexed as

AnimalsBinding SitesCalciumConsensus SequenceCyclic AMP-Dependent Protein KinasesElectrophysiologyMicePhosphorylationPotassium ChannelsProtein IsoformsProtein Structure, QuaternaryProtein SubunitsCalciumCyclic AMP-Dependent Protein KinasesPotassium ChannelsProtein IsoformsProtein Subunits

Identifiers

PMID15280542
PMCPMC511071
OpenAlexW2146575670

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.