Evidence map›Paper›PMID 15243742›Full record

ArticlePflugers Archiv : European journal of physiology2004

Protein kinase A inhibits intermediate conductance Ca2+-activated K+ channels expressed in Xenopus oocytes.

Craig B Neylon, Theresa D'Souza, Peter H Reinhart

Abstract read
PubMed Publisher
In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

12 citing papers in PubMed, 27 citations in OpenAlex.

  1. Protein Kinase A-Mediated Suppression of the Slow Afterhyperpolarizing KCa3.1 Current in Temporal Lobe Epilepsy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  2. Review
  3. Activity-Dependent Facilitation of CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  4. Article
  5. Article
  6. PKA reduces the rat and human KCa3.1 current, CaM binding, and Ca2+ signaling, which requires Ser332/334 in the CaM-binding C terminus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
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 3 institutions in 2 countries.

Craig B NeylonDepartment of Neurobiology, Duke University Medical Center, P.O. Box 3209, Durham, NC, USA.
Theresa D'Souza
Peter H Reinhart
Duke Medical Center · USDuke University · USDuke University Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intermediate-conductance (IK) Ca(2+)-activated K(+) channels are expressed in many different cell types where they perform a variety of functions including cell volume regulation, transepithelial secretion, lymphocyte activation and cell cycle progression. IK channels are thought to be regulated by phosphorylation; however, whether kinases act directly on the channel is unclear. Using IK channels heterologously expressed in Xenopus oocytes, we demonstrate that IK channels are potently inhibited (60%) by the catalytic subunit of protein kinase A (PKA). Inhibition of IK channel current by PKA is abolished by mutation of four phosphorylation residues (S312, T327, S332, and T348) in the putative calmodulin-binding region of the channel. Evidence for direct modulation of the IK channel by PKA was further demonstrated using GST fusion proteins. The major site of phosphorylation was found to be serine 332; however, other residues were also phosphorylated. We conclude that IK channels can be directly regulated by the cAMP second-messenger system. The mechanism appears to involve direct phosphorylation by PKA of a modulatory locus in the cytoplasmic region of the channel, the site at which calmodulin is thought to interact. Modulation of IK channels by protein kinases may be an important mechanism regulating cell function.

Indexed as

Amino Acid SequenceAnimalsConsensus SequenceCyclic AMP-Dependent Protein KinasesElectric ConductivityGene ExpressionGlutathioneIn Vitro TechniquesMolecular Sequence DataMutagenesisOocytesPhosphorylationPotassium Channels, Calcium-ActivatedRecombinant Fusion ProteinsXenopusCyclic AMP-Dependent Protein KinasesGlutathionePotassium Channels, Calcium-ActivatedRecombinant Fusion Proteins

Identifiers

PMID15243742
OpenAlexW2082633548

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.