Evidence map›Paper›PMID 7831317›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

An autoregulatory region in protein kinase C: the pseudoanchoring site.

D Ron, D Mochly-Rosen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

66 citing papers in PubMed, 198 citations in OpenAlex.

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  7. Fluvastatin inhibits Rab5-mediated IKs internalization caused by chronic CaJournal of molecular and cellular cardiology · 2019
    Article
  8. Rice black-streaked dwarf virus P10 suppresses protein kinase C in insect vector through changing the subcellular localization of LsRACK1.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Article
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6 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

2 authors at 1 institution in 1 country.

D RonDepartment of Molecular Pharmacology, Stanford University, School of Medicine, CA 94305-5332.
D Mochly-Rosen
Stanford University · US

Funding

RULES OF PROTEIN KINASE IN CARDIAC MYOCYTESR01HL043380 · NHLBI · STANFORD UNIVERSITY · PI MOCHLY-ROSEN, DARIA · 1989 to 1996
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NHLBI NIH HHS R01 HL-43380
6 · The paper itself

Abstract

We have previously identified receptors for activated C kinase (RACKs) as components of protein kinase C (PKC) signaling. RACK1, a recently cloned 36-kDa RACK, has short sequences of homology to PKC. A possible explanation for the homologous sequences between the ligand (PKC) and its intracellular receptor (RACK1) may be that, similar to the pseudosubstrate autoregulatory sequence on PKC, there is also a pseudo-RACK1 binding site on the enzyme. If this is the case, peptides with these sequences (derived from either RACK1 or PKC) are expected to affect PKC binding to RACK1 in vitro and PKC-mediated functions in vivo. Here, we show that the PKC-derived peptide (pseudo-RACK1 peptide), but not its RACK1 homologue, modulated PKC function both in vitro and in vivo. Our data suggest that the pseudo-RACK1 peptide binds and activates PKC in the absence of PKC activators and thereby acts as an agonist of PKC function in vivo. Therefore, the pseudo-RACK1 sequence in PKC appears to be another autoregulatory site; when PKC is in an inactive conformation, the pseudo-RACK1 site interacts with the RACK-binding site. Activation of PKC exposes the RACK-binding site, enabling the association of the enzyme with its anchoring RACK. Similar pseudoanchoring sites may regulate the function of other protein kinases.

Indexed as

Amino Acid SequenceAnimalsBinding SitesEnzyme ActivationInsulinIsoenzymesMicroinjectionsModels, BiologicalModels, MolecularMolecular Sequence DataOocytesPeptidesProtein Kinase CReceptors, Cell SurfaceReceptors for Activated C KinaseRecombinant ProteinsInsulinIsoenzymespeptide IPeptidesProtein Kinase CReceptors, Cell SurfaceReceptors for Activated C KinaseRecombinant Proteins

Identifiers

PMID7831317
PMCPMC42767
OpenAlexW2034134605

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.