Evidence map›Paper›PMID 22487381›Full record

ArticleJournal of molecular and cellular cardiology2012

PKA phosphorylation of cardiac ryanodine receptor modulates SR luminal Ca2+ sensitivity.

Nina D Ullrich, Héctor H Valdivia, Ernst Niggli

Abstract read
In one paragraph

Article in Journal of molecular and cellular cardiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. RyR2 phosphorylation alters dyad architecture.The Journal of general physiology · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Cellular Mechanisms Underlying the Low Cardiotoxicity of Istaroxime.Journal of the American Heart Association · 2021
    Article
  12. TRIC-A regulates intracellular CaPflugers Archiv : European journal of physiology · 2021
    Review
  13. Article
  14. Review
  15. Review
  16. Calcium Signaling in Cardiomyocyte Function.Cold Spring Harbor perspectives in biology · 2020
    Review
  17. Article
  18. Molecular Mechanisms Mediating Adaptation to Exercise.Advances in experimental medicine and biology · 2020
    Review
  19. Disruption of CaCirculation · 2019
    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

3 authors at 2 institutions in 2 countries.

Nina D UllrichDepartment of Physiology, University of Bern, Bühlplatz 5, CH-3012 Bern, Switzerland.
Héctor H Valdivia
Ernst Niggli
University of Bern · CHUniversity of Wisconsin–Madison · US

Funding

RYANODINE RECEPTORS, Ca2+-TRIGGERED ARRHYTHMIAS AND HCMP01HL094291 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MOSS, RICHARD L · 2009 to 2013
$9.7M
Ryanodine Receptors, Calcium-dependent Arrhythmias & HCMR01HL055438 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI VALDIVIA, HECTOR H · 1996 to 2023
$8.0M
NHLBI NIH HHS P01 HL094291NHLBI NIH HHS P01-HL094291NHLBI NIH HHS R01 HL055438NHLBI NIH HHS R01-HL055438
6 · The paper itself

Abstract

During physical exercise and stress, the sympathetic system stimulates cardiac contractility via β-adrenergic receptor activation, resulting in protein kinase A (PKA)-mediated phosphorylation of the cardiac ryanodine receptor, RyR2, at Ser2808. Hyperphosphorylation of RyR2-S2808 has been proposed as a mechanism contributing to arrhythmogenesis and heart failure. However, the role of RyR2 phosphorylation during β-adrenergic stimulation remains controversial. We examined the contribution of RyR2-S2808 phosphorylation to altered excitation-contraction coupling and Ca(2+) signaling using an experimental approach at the interface of molecular and cellular levels and a transgenic mouse with ablation of the RyR2-S2808 phosphorylation site (RyR2-S2808A). Experimentally challenging the communication between L-type Ca(2+) channels and RyR2 led to a spatiotemporal de-synchronization of RyR2 openings, as visualized using confocal Ca(2+) imaging. β-Adrenergic stimulation re-synchronized RyR2s, but less efficiently in RyR2-S2808A than in control cardiomyocytes, as indicated by comprehensive analysis of RyR2 activation. In addition, spontaneous Ca(2+) waves in RyR2-S2808A myocytes showed significantly slowed propagation and complete absence of acceleration during β-adrenergic stress, unlike wild type cells. Single channel recordings revealed an attenuation of luminal Ca(2+) sensitivity in RyR2-S2808A channels upon addition of PKA. This suggests that phosphorylation of RyR2-S2808 may be involved in RyR2 modulation by luminal (intra-SR) Ca(2+) ([Ca(2+)](SR)). We show here by three independent experimental approaches that PKA-dependent RyR2-S2808 phosphorylation plays significant functional roles at the subcellular level, namely, Ca(2+) release synchronization, Ca(2+) wave propagation and functional adaptation of RyR2 to variable [Ca(2+)](SR). These results indicate a direct mechanistic link between RyR2 phosphorylation and SR luminal Ca(2+) sensing.

Indexed as

Adrenergic beta-AgonistsAnimalsCalciumCyclic AMP-Dependent Protein KinasesDiastoleExcitation Contraction CouplingLipid BilayersMiceMice, TransgenicMyocardial ContractionMyocytes, CardiacPhosphorylationRyanodine Receptor Calcium Release ChannelSarcoplasmic ReticulumAdrenergic beta-AgonistsCalciumCyclic AMP-Dependent Protein KinasesLipid BilayersRyanodine Receptor Calcium Release Channel

Identifiers

PMID22487381
PMCPMC3674825
OpenAlexW2009054667

What OpenQuestion holds

Textmetadata
LicenceTDM
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.