Evidence map›Paper›PMID 24509862›Full record

ArticleThe Journal of biological chemistry2014

Regulation of the skeletal muscle ryanodine receptor/Ca2+-release channel RyR1 by S-palmitoylation.

Ruchi Chaube, Douglas T Hess, Ya-Juan Wang, Bradley Plummer, Qi-An Sun, Kennneth Laurita, Jonathan S Stamler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Role of RONS and eIFs in Cancer Progression.Oxidative medicine and cellular longevity · 2021
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review of RyR1 pathway and associated pathomechanisms.Acta neuropathologica communications · 2016
    Review
  14. Article
  15. ROS and ROS-Mediated Cellular Signaling.Oxidative medicine and cellular longevity · 2016
    Review
  16. Malignant hyperthermia: a review.Orphanet journal of rare diseases · 2015
    Review
  17. Review
  18. S-palmitoylation and s-oleoylation of rabbit and pig sarcolipin.The Journal of biological chemistry · 2014
    Article
  19. Review
  20. Ion channel regulation by protein S-acylation.The Journal of general physiology · 2014
    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

7 authors at 3 institutions in 1 country.

Ruchi ChaubeFrom the Institute for Transformative Molecular Medicine and Department of Medicine, Case Western Reserve University School of Medicine and University Hospitals, Cleveland, Ohio 44106.
Douglas T Hess
Ya-Juan Wang
Bradley Plummer
Qi-An Sun
Kennneth Laurita
Jonathan S Stamler
Case Western Reserve University · USUniversity School · USMetroHealth Medical Center · US

Funding

BIOMETRIC-GENETIC ANALYSIS OF CARDIOVASCULAR DISEASET32HL007567 · NHLBI · LOUISIANA STATE UNIV HSC NEW ORLEANS · PI ZHU, XIAOFENG · 1985 to 2021
$6.0M
SARCOPLASMIC RETICULUM FUNCTION AND REASSEMBLYR01AR018687 · NIAMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MEISSNER, GERHARD W · 1986 to 2009
$3.9M
NHLBI NIH HHS R01 HL0591130NHLBI NIH HHS T32 HL007567NIAMS NIH HHS R01 AR018687
6 · The paper itself

Abstract

The ryanodine receptor/Ca(2+)-release channels (RyRs) of skeletal and cardiac muscle are essential for Ca(2+) release from the sarcoplasmic reticulum that mediates excitation-contraction coupling. It has been shown that RyR activity is regulated by dynamic post-translational modifications of Cys residues, in particular S-nitrosylation and S-oxidation. Here we show that the predominant form of RyR in skeletal muscle, RyR1, is subject to Cys-directed modification by S-palmitoylation. S-Palmitoylation targets 18 Cys within the N-terminal, cytoplasmic region of RyR1, which are clustered in multiple functional domains including those implicated in the activity-governing protein-protein interactions of RyR1 with the L-type Ca(2+) channel CaV1.1, calmodulin, and the FK506-binding protein FKBP12, as well as in "hot spot" regions containing sites of mutations implicated in malignant hyperthermia and central core disease. Eight of these Cys have been identified previously as subject to physiological S-nitrosylation or S-oxidation. Diminishing S-palmitoylation directly suppresses RyR1 activity as well as stimulus-coupled Ca(2+) release through RyR1. These findings demonstrate functional regulation of RyR1 by a previously unreported post-translational modification and indicate the potential for extensive Cys-based signaling cross-talk. In addition, we identify the sarco/endoplasmic reticular Ca(2+)-ATPase 1A and the α1S subunit of the L-type Ca(2+) channel CaV1.1 as S-palmitoylated proteins, indicating that S-palmitoylation may regulate all principal governors of Ca(2+) flux in skeletal muscle that mediates excitation-contraction coupling.

Indexed as

Protein Processing, Post-TranslationalAnimalsCalciumCells, CulturedHumansMiceMice, Inbred C57BLMuscle, SkeletalPalmitic AcidRabbitsRyanodine Receptor Calcium Release ChannelCalciumPalmitic AcidRyanodine Receptor Calcium Release ChannelCalcium Intracellular ReleasePost-translational ModificationProtein PalmitoylationRyanodine ReceptorSkeletal Muscle

Identifiers

PMID24509862
PMCPMC3961684
OpenAlexW2087823822

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.