Evidence map›Paper›PMID 14983009›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

RACK1 binds to inositol 1,4,5-trisphosphate receptors and mediates Ca2+ release.

Randen L Patterson, Damian B van Rossum, Roxanne K Barrow, Solomon H Snyder

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. The T-type calcium channelosome.Pflugers Archiv : European journal of physiology · 2024
    Review
  4. Molecular mechanisms of alcohol's effects on the human body: A review and update.Journal of biochemical and molecular toxicology · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Signaling pathways mediating alcohol effects.Current topics in behavioral neurosciences · 2013
    Review
  14. Inositol trisphosphate receptors in smooth muscle cells.American journal of physiology. Heart and circulatory physiology · 2012
    Review
  15. Article
  16. Article
  17. Review
  18. RACK1, A multifaceted scaffolding protein: Structure and function.Cell communication and signaling : CCS · 2011
    Article
  19. 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

4 authors.

Randen L PattersonDepartment of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Damian B van Rossum
Roxanne K Barrow
Solomon H Snyder

Funding

UNDERSTANDING NO SIGNALING RESULTING IN NEUROPROTECTION.P50DA000266 · NIDA · JOHNS HOPKINS UNIVERSITY · PI WORLEY, PAUL F · 1985 to 2017
$45.2M
NEUROCHEMICAL ACTIONS OF PSYCHOTROPIC DRUGSR37MH018501 · NIMH · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1990 to 2009
$11.5M
NEUROCHEMICAL ACTIONS OF PSYCHOTROPIC DRUGSR01MH018501 · NIMH · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1985 to 2019
$10.8M
NEUROTRANSMITTER RECEPTORSK05DA000074 · NIDA · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1985 to 2009
$1.3M
NIDA NIH HHS DA-000266NIDA NIH HHS DA-00074NIDA NIH HHS K05 DA000074NIDA NIH HHS P50 DA000266NIH HHS NH65090NIMH NIH HHS MH-18501NIMH NIH HHS R01 MH018501NIMH NIH HHS R37 MH018501
6 · The paper itself

Abstract

RACK1 is not a G protein but closely resembles the heterotrimeric Gbeta-subunit. RACK1 serves as a scaffold, linking protein kinase C to its substrates. We demonstrate that RACK1 physiologically binds inositol 1,4,5-trisphosphate receptors and regulates Ca2+ release by enhancing inositol 1,4,5-trisphosphate receptor binding affinity for inositol 1,4,5-trisphosphate. Overexpression of RACK1 or depletion of RACK1 by interference RNA markedly augments or diminishes Ca2+ release, respectively, without affecting Ca2+ entry. These findings establish RACK1 as a physiologic mediator of agonist-induced Ca2+ release.

Indexed as

Amino Acid SubstitutionAnimalsCalciumCalcium ChannelsCalcium SignalingCell LineGTP-Binding ProteinsHumansInositol 1,4,5-Trisphosphate ReceptorsKidneyKineticsMutagenesis, Site-DirectedNeoplasm ProteinsPC12 CellsProtein BindingRatsCalciumCalcium ChannelsGTP-Binding ProteinsInositol 1,4,5-Trisphosphate ReceptorsITPR1 protein, humanNeoplasm ProteinsRACK1 protein, humanReceptors, Cell SurfaceReceptors, Cytoplasmic and NuclearReceptors for Activated C KinaseRecombinant ProteinsRNA, Small Interfering

Identifiers

PMID14983009
PMCPMC356950

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.