Evidence map›Paper›PMID 14561822›Full record

ArticleThe Journal of physiology2003

Conditional protein phosphorylation regulates BK channel activity in rat cerebellar Purkinje neurons.

Hélène A Widmer, Iain C M Rowe, Michael J Shipston

Abstract read
In one paragraph

Article in The Journal of physiology, 2003. 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
1.1field-weighted citation impact, top 24% 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, 52 citations in OpenAlex.

  1. CaInternational journal of molecular sciences · 2023
    Review
  2. Protein kinase Cγ in cerebellar Purkinje cells regulates CaProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Article
  4. Cereblon in health and disease.Pflugers Archiv : European journal of physiology · 2016
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Stochastic calcium mechanisms cause dendritic calcium spike variability.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Dual role of protein kinase C on BK channel regulation.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  17. Article
  18. Article
  19. Article
  20. The BK-mediated fAHP is modulated by learning a hippocampus-dependent task.Proceedings of the National Academy of Sciences of the United States of America · 2008
    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

3 authors at 2 institutions in 1 country.

Hélène A WidmerMembrane Biology Group, Division of Biomedical Science, University of Edinburgh, Hugh Robson Building, Edinburgh EH8 9XD, Scotland, UK.
Iain C M Rowe
Michael J Shipston
University of Edinburgh · GBRobert Gordon University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Large conductance calcium- and voltage-activated potassium (BK) channels are widely expressed in the mammalian central nervous system. Although the activity of BK channels in endocrine and vascular cells is regulated by protein kinases and phosphatases associated with the channel complex, direct evidence for such modulation in neurons is largely lacking. Single-channel analysis from inside-out patches isolated from the soma of dissociated rat cerebellar Purkinje neurons demonstrated that the activity of BK channels is regulated by multiple endogenous protein kinases and protein phosphatases in the membrane patch. The majority of BK channels were non-inactivating and displayed a 'low' activity phenotype determined at +40 mV and 1 muM intracellular free calcium. These channels were activated by cAMP-dependent protein kinase (PKA) associated with the patch and the extent of PKA activation was limited by an opposing endogenous type 2A-like protein phosphatase (PP2A). Importantly, PKA activation was dependent upon the prior phosphorylation status of the BK channel complex dynamically controlled by protein kinase C (PKC) and protein phosphatase 1 (PP1). In contrast, Purkinje cells also displayed a low proportion of non-inactivating BK channels with a 'high' activity under the same recording conditions and these channels were inhibited by endogenous PKA. Our data suggest that: (1) multiple endogenous protein kinases and phosphatases functionally couple to the BK channel complex to allow conditional modulation of BK channel activity in neurons, and (2) native, phenotypically distinct, neuronal BK channels are differentially sensitive to PKA-dependent phosphorylation.

Indexed as

AnimalsCerebellumCyclic AMPCyclic AMP-Dependent Protein KinasesElectrophysiologyLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsNerve Tissue ProteinsPatch-Clamp TechniquesPhenotypePhosphoprotein PhosphatasesPhosphorylationPotassium Channel BlockersPotassium Channels, Calcium-ActivatedProtein Phosphatase 1Purkinje CellsCyclic AMPCyclic AMP-Dependent Protein KinasesLarge-Conductance Calcium-Activated Potassium ChannelsNerve Tissue ProteinsPhosphoprotein PhosphatasesPotassium Channel BlockersPotassium Channels, Calcium-ActivatedProtein Phosphatase 1

Identifiers

PMID14561822
PMCPMC2343377
OpenAlexW2066992617

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.