Evidence map›Paper›PMID 29294329›Full record

ArticleJournal of molecular and cellular cardiology2018

β-Adrenergic regulation of cardiac type 2A protein phosphatase through phosphorylation of regulatory subunit B56δ at S573.

Antonella Ranieri, Elizabeth Kemp, Joseph R Burgoyne, Metin Avkiran

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular and cellular cardiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
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  12. Regulation of Cardiac PKA Signaling by cAMP and Oxidants.Antioxidants (Basel, Switzerland) · 2021
    Review
  13. Article
  14. The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  15. 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

4 authors at 2 institutions in 1 country.

Antonella RanieriSchool of Cardiovascular Medicine and Sciences, King's College London British Heart Foundation Centre of Research Excellence, The Rayne Institute, St Thomas' Hospital, London, United Kingdom.
Elizabeth KempSchool of Cardiovascular Medicine and Sciences, King's College London British Heart Foundation Centre of Research Excellence, The Rayne Institute, St Thomas' Hospital, London, United Kingdom.
Joseph R BurgoyneSchool of Cardiovascular Medicine and Sciences, King's College London British Heart Foundation Centre of Research Excellence, The Rayne Institute, St Thomas' Hospital, London, United Kingdom.
Metin AvkiranSchool of Cardiovascular Medicine and Sciences, King's College London British Heart Foundation Centre of Research Excellence, The Rayne Institute, St Thomas' Hospital, London, United Kingdom. Electronic address: metin.avkiran@kcl.ac.uk.
King's College London · GBBritish Heart Foundation · GB

Funding

British Heart Foundation FS/14/1/30551British Heart Foundation PG/12/48/29638
6 · The paper itself

Abstract

backgroundType 2A protein phosphatase (PP2A) enzymes are serine/threonine phosphatases which comprise a scaffold A subunit, a regulatory B subunit and a catalytic C subunit, and have been implicated in the dephosphorylation of multiple cardiac phosphoproteins. B subunits determine subcellular targeting, substrate specificity and catalytic activity, and can themselves be regulated by post-translational modifications. We explored potential β-adrenergic regulation of PP2A in cardiomyocytes through phosphorylation of the regulatory B subunit isoform B56δ. METHODS AND

resultsPhosphate affinity SDS-PAGE and immunoblot analysis revealed increased phosphorylation of B56δ in adult rat ventricular myocytes (ARVM) exposed to the β-adrenergic receptor (βAR) agonist isoprenaline (ISO). Phosphorylation of B56δ occurred at S573, primarily through stimulation of the β

conclusionsIn cardiomyocytes, βAR stimulation induces PKA-mediated phosphorylation of the PP2A regulatory subunit isoform B56δ at S573, which increases associated PP2A catalytic activity. This is likely to regulate the phosphorylation status of specific B56δ-PP2A substrates, which remain to be identified.

Indexed as

AdenoviridaeAdrenergic beta-AgonistsAmino Acid SequenceAnimalsCardiomegalyDisease Models, AnimalHEK293 CellsHumansIsoproterenolMaleMiceMyocardiumPhosphoproteinsPhosphorylationPhosphoserineProtein Phosphatase 2Adrenergic beta-AgonistsIsoproterenolPhosphoproteinsPhosphoserinePPP2R5D protein, humanPpp2r5d protein, ratProtein Phosphatase 2Protein SubunitsB56δCardiomyocytesPhosphatasePhosphorylationProtein kinase A (PKA)Type 2A protein phosphatase (PP2A)β-Adrenergic signaling

Identifiers

PMID29294329
PMCPMC5823843
OpenAlexW2777006222

What OpenQuestion holds

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Registered trials

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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.