Evidence map›Paper›PMID 11720989›Full record

ArticleBiophysical journal2001

Characteristics of irreversible ATP activation suggest that native skeletal ryanodine receptors can be phosphorylated via an endogenous CaMKII.

A F Dulhunty, D Laver, S M Curtis, S Pace, C Haarmann, E M Gallant

Abstract read
In one paragraph

Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Trial
  2. CaMKII as a Therapeutic Target in Cardiovascular Disease.Annual review of pharmacology and toxicology · 2023
    Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Exercise and fatigue.Sports medicine (Auckland, N.Z.) · 2009
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

6 authors.

A F DulhuntyMuscle Research Group, John Curtin School of Medical Research, Canberra, ACT 2601, Australia. angela.dulhunty@anu.edu.au
D Laver
S M Curtis
S Pace
C Haarmann
E M Gallant

Funding

RYR ACCESSORY PROTEINS AND MALIGNANT HYPERTHERMIAF33AR008477 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI PALMER, ESTHER G · 1997 to 1997
–
NIAMS NIH HHS AR08477
6 · The paper itself

Abstract

Phosphorylation of skeletal muscle ryanodine receptor (RyR) calcium release channels by endogenous kinases incorporated into lipid bilayers with native sarcoplasmic reticulum vesicles was investigated during exposure to 2 mM cytoplasmic ATP. Activation of RyRs after 1-min exposure to ATP was reversible upon ATP washout. In contrast, activation after 5 to 8 min was largely irreversible: the small fall in activity with washout was significantly less than that after brief ATP exposure. The irreversible activation was reduced by acid phosphatase and was not seen after exposure to nonhydrolyzable ATP analogs. The data suggested that the channel complex was phosphorylated after addition of ATP and that phosphorylation reduced the RyR's sensitivity to ATP, adenosine, and Ca(2+). The endogenous kinase was likely to be a calcium calmodulin kinase II (CaMKII) because the CaMKII inhibitor KN-93 and an inhibitory peptide for CaMKII prevented the phosphorylation-induced irreversible activation. In contrast, phosphorylation effects remained unchanged with inhibitory peptides for protein kinase C and A. The presence of CaMKIIbeta in the SR vesicles was confirmed by immunoblotting. The results suggest that CaMKII is anchored to skeletal muscle RyRs and that phosphorylation by this kinase alters the enhancement of channel activity by ATP and Ca(2+).

Indexed as

Acid PhosphataseAdenosineAdenosine TriphosphateAdenylyl ImidodiphosphateAllelesAnimalsBinding, CompetitiveCaffeineCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Central Nervous System StimulantsDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelElectrophysiologyImmunoblottingLigands5'-adenylyl (beta,gamma-methylene)diphosphonateAcid PhosphataseAdenosineAdenosine TriphosphateAdenylyl ImidodiphosphateCaffeineCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Central Nervous System StimulantsLigandsLipid BilayersPeptidesProtein Kinase CRyanodine Receptor Calcium Release Channel

Identifiers

PMID11720989
PMCPMC1301783

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.