Evidence map›Paper›PMID 21209098›Full record

ArticleThe Journal of biological chemistry2011

Selective expression in carotid body type I cells of a single splice variant of the large conductance calcium- and voltage-activated potassium channel confers regulation by AMP-activated protein kinase.

Fiona A Ross, J Nicole Rafferty, Mark L Dallas, Oluseye Ogunbayo, Naoko Ikematsu, Heather McClafferty, Lijun Tian, Helene Widmer, Iain C M Rowe, Christopher N Wyatt and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
3.2field-weighted citation impact, top 8% 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, 65 citations in OpenAlex.

  1. Review
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  10. AMPK and the Need to Breathe and Feed: What's the Matter with Oxygen?International journal of molecular sciences · 2020
    Review
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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

14 authors at 5 institutions in 2 countries.

Fiona A RossCollege of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, United Kingdom.
J Nicole Rafferty
Mark L Dallas
Oluseye Ogunbayo
Naoko Ikematsu
Heather McClafferty
Lijun Tian
Helene Widmer
Iain C M Rowe
Christopher N Wyatt
Michael J Shipston
Chris Peers
D Grahame Hardie
A Mark Evans
University of Edinburgh · GBUniversity of Dundee · GBUniversity of Leeds · GBGlasgow Caledonian University · GBWright State University · US

Funding

Wellcome Trust 080982Wellcome Trust 082407Wellcome Trust 81195
6 · The paper itself

Abstract

Inhibition of large conductance calcium-activated potassium (BKCa) channels mediates, in part, oxygen sensing by carotid body type I cells. However, BKCa channels remain active in cells that do not serve to monitor oxygen supply. Using a novel, bacterially derived AMP-activated protein kinase (AMPK), we show that AMPK phosphorylates and inhibits BKCa channels in a splice variant-specific manner. Inclusion of the stress-regulated exon within BKCa channel α subunits increased the stoichiometry of phosphorylation by AMPK when compared with channels lacking this exon. Surprisingly, however, the increased phosphorylation conferred by the stress-regulated exon abolished BKCa channel inhibition by AMPK. Point mutation of a single serine (Ser-657) within this exon reduced channel phosphorylation and restored channel inhibition by AMPK. Significantly, RT-PCR showed that rat carotid body type I cells express only the variant of BKCa that lacks the stress-regulated exon, and intracellular dialysis of bacterially expressed AMPK markedly attenuated BKCa currents in these cells. Conditional regulation of BKCa channel splice variants by AMPK may therefore determine the response of carotid body type I cells to hypoxia.

Indexed as

AMP-Activated Protein KinasesAnimalsAnimals, NewbornCarotid BodyElectrophysiologyHEK293 CellsHumansLarge-Conductance Calcium-Activated Potassium ChannelsLiverMicePhosphorylationProtein IsoformsRatsReverse Transcriptase Polymerase Chain ReactionAMP-Activated Protein KinasesLarge-Conductance Calcium-Activated Potassium ChannelsProtein Isoforms

Identifiers

PMID21209098
PMCPMC3069395
OpenAlexW2052458266

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.