Evidence map›Paper›PMID 10508860›Full record

ArticleThe Journal of cell biology1999

Presenilin 1 suppresses the function of c-Jun homodimers via interaction with QM/Jif-1.

I Imafuku, T Masaki, M Waragai, S Takeuchi, M Kawabata, S Hirai, S Ohno, L E Nee, C F Lippa, I Kanazawa and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
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  5. Hallmarks of ribosomopathies.Nucleic acids research · 2020
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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

12 authors at 7 institutions in 2 countries.

I ImafukuDepartment of Neurology, Graduate School of Medicine, University of Tokyo, Tokyo 113-8655, Japan.
T Masaki
M Waragai
S Takeuchi
M Kawabata
S Hirai
S Ohno
L E Nee
C F Lippa
I Kanazawa
M Imagawa
H Okazawa
The University of Tokyo · JPYokohama City University · JPHahnemann University Hospital · USJapanese Foundation For Cancer Research · JPNational Defense Medical College · JPNational Institutes of Health · USOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Presenilin 1 (PS1) is the causative gene for an autosomal dominant familial Alzheimer's disease (AD) mapped to chromosome 14. Here we show that QM/Jun-interacting factor (Jif)-1, a negative regulator of c-Jun, is a candidate to mediate the function of PS1 in the cell. We screened for proteins that bind to PS1 from a human embryonic brain cDNA library using the two-hybrid method and isolated one clone encoding the QM/Jif-1 gene. The binding of QM/Jif-1 to full-length PS1 was confirmed in vitro by pull-down assay, and in vivo by immunoprecipitation assays with human samples, including AD brains. Immunoelectronmicroscopic analysis showed that QM/Jif-1 and PS1 are colocalized at the endoplasmic reticulum, and the nuclear matrix in human brain neurons. Chloramphenicol acetyltransferase assays in F9 cells showed that PS1 suppresses transactivation by c-Jun/c-Jun but not by c-Jun/c-Fos heterodimers, consistent with the reported function of QM/Jif-1. By monitoring fluorescent recombinant protein and by gel mobility shift assays, PS1 was shown to accelerate the translocation of QM from the cytoplasm to the nucleus and to thereby suppress the binding of c-Jun homodimer to 12-O-tetradecanoylphorbol-13- acetate (TPA)-responsive element (TRE). PS1 suppressed c-jun-associated apoptosis by retinoic acid in F9 embryonic carcinoma cells, whereas this suppression of apoptosis is attenuated by mutation in PS1. Collectively, the novel function of PS1 via QM/Jif-1 influences c-jun-mediated transcription and apoptosis.

Indexed as

Ribosomal ProteinsAdultAlzheimer DiseaseAmino Acid SequenceAnimalsApoptosisBiological TransportBrainCarrier ProteinsCell NucleusDimerizationFemaleHumansMembrane ProteinsMiceMolecular Sequence DataCarrier ProteinsMembrane ProteinsPresenilin-1Proto-Oncogene Proteins c-junPSEN1 protein, humanRibosomal ProteinsRNA, MessengerRPL10 protein, humanRpl10 protein, mouse

Identifiers

PMID10508860
PMCPMC2164975
OpenAlexW2119228169

What OpenQuestion holds

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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.