Evidence map›Paper›PMID 11352932›Full record

ArticleThe Journal of cell biology2001

Phosphorylation-dependent regulation of ryanodine receptors: a novel role for leucine/isoleucine zippers.

S O Marx, S Reiken, Y Hisamatsu, M Gaburjakova, J Gaburjakova, Y M Yang, N Rosemblit, A R Marks

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

125 citing papers in PubMed, 290 citations in OpenAlex.

  1. The RyR-like-FKBP12-PKA Complex Regulates Intracellular CaInternational journal of molecular sciences · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Targeting p21-activated kinase 1 for development of a novel anti-arrhythmic drug class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  10. Review
  11. Targeting ryanodine receptors to treat human diseases.The Journal of clinical investigation · 2023
    Review
  12. Role of CaArchives of toxicology · 2023
    Review
  13. A perinuclear calcium compartment regulates cardiac myocyte hypertrophy.Journal of molecular and cellular cardiology · 2022
    Article
  14. Ryanodine receptor RyR1-mediated elevation of CaJournal of animal science and biotechnology · 2022
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. TRIC-A regulates intracellular CaPflugers Archiv : European journal of physiology · 2021
    Review
  20. Article

65 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

S O MarxCenter for Molecular Cardiology, Department of Medicine, College of Physicians and Surgeons of Columbia University, 630 West 168th St., New York, NY 10032, USA.
S Reiken
Y Hisamatsu
M Gaburjakova
J Gaburjakova
Y M Yang
N Rosemblit
A R Marks
Columbia University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ryanodine receptors (RyRs), intracellular calcium release channels required for cardiac and skeletal muscle contraction, are macromolecular complexes that include kinases and phosphatases. Phosphorylation/dephosphorylation plays a key role in regulating the function of many ion channels, including RyRs. However, the mechanism by which kinases and phosphatases are targeted to ion channels is not well understood. We have identified a novel mechanism involved in the formation of ion channel macromolecular complexes: kinase and phosphatase targeting proteins binding to ion channels via leucine/isoleucine zipper (LZ) motifs. Activation of kinases and phosphatases bound to RyR2 via LZs regulates phosphorylation of the channel, and disruption of kinase binding via LZ motifs prevents phosphorylation of RyR2. Elucidation of this new role for LZs in ion channel macromolecular complexes now permits: (a) rapid mapping of kinase and phosphatase targeting protein binding sites on ion channels; (b) predicting which kinases and phosphatases are likely to regulate a given ion channel; (c) rapid identification of novel kinase and phosphatase targeting proteins; and (d) tools for dissecting the role of kinases and phosphatases as modulators of ion channel function.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCalcium ChannelsCarrier ProteinsCyclic AMP-Dependent Protein KinasesDogsIsoleucineLeucine ZippersMembrane ProteinsMolecular Sequence DataMutagenesis, Site-DirectedMyocardiumPhosphoprotein PhosphatasesPhosphorylationRyanodine Receptor Calcium Release ChannelCalcium ChannelsCarrier ProteinsCyclic AMP-Dependent Protein KinasesIsoleucineMembrane ProteinsPhosphoprotein PhosphatasesRyanodine Receptor Calcium Release Channel

Identifiers

PMID11352932
PMCPMC2192391
OpenAlexW2065693120

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.