Evidence map›Paper›PMID 8302854›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins.

D Ron, C H Chen, J Caldwell, L Jamieson, E Orr, D Mochly-Rosen

Erratum issuedOpen access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 277 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
277citing papers in PubMed, 1 pooled it
12.6field-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

277 citing papers in PubMed, 1 synthesis or guideline pooled it, 721 citations in OpenAlex.

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  20. RACK1 promotes the occurrence and progression of cervical carcinoma.Journal of clinical laboratory analysis · 2024
    Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

D RonDepartment of Molecular Pharmacology, Stanford University School of Medicine, CA 94305-5332.
C H Chen
J Caldwell
L Jamieson
E Orr
D Mochly-Rosen
Stanford University · USUniversity of Leicester · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Protein kinase C (PKC) translocates from the soluble to the cell particulate fraction on activation. Intracellular receptors that bind activated PKC in the particulate fraction have been implicated by a number of studies. Previous work identified 30- to 36-kDa proteins in the particulate fraction of heart and brain that bound activated PKC in a specific and saturable manner. These proteins were termed receptors for activated C-kinase, or RACKs. In the following study, we describe the cloning of a cDNA encoding a 36-kDa protein (RACK1) that fulfills the criteria for RACKs. (i) RACK1 bound PKC in the presence of PKC activators, but not in their absence. (ii) PKC binding to the recombinant RACK1 was not inhibited by a pseudosubstrate peptide or by a substrate peptide derived from the pseudosubstrate sequence, indicating that the binding did not reflect simply PKC association with its substrate. (iii) Binding of PKC to RACK1 was saturable and specific; two other protein kinases did not bind to RACK1. (iv) RACK1 contains two short sequences homologous to a PKC binding sequence previously identified in annexin I and in the brain PKC inhibitor KCIP. Peptides derived from these sequences inhibited PKC binding to RACK1. Finally, RACK1 is a homolog of the beta subunit of G proteins, which were recently implicated in membrane anchorage of the beta-adrenergic receptor kinase [Pitcher, J., Inglese, L., Higgins, J. B., Arriza, J. A., Casey, P. J., Kim, C., Benovic, J. L., Kwatra, M. M., Caron, M. G. & Lefkowitz, R. J. (1992) Science 257, 1264-1267]. Our in vitro data suggest a role for RACK1 in PKC-mediated signaling.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBinding SitesBrainCloning, MolecularDNA, ComplementaryEscherichia coliGTP-Binding ProteinsIn Vitro TechniquesMolecular Sequence DataProtein BindingProtein Kinase CRatsRats, Sprague-DawleyReceptors, Cell SurfaceDNA, ComplementaryGTP-Binding ProteinsProtein Kinase CReceptors, Cell SurfaceReceptors for Activated C Kinase

Identifiers

PMID8302854
PMCPMC521407
OpenAlexW2160332942

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.