Evidence map›Paper›PMID 9724731›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase.

R Ferreira, L Magnaghi-Jaulin, P Robin, A Harel-Bellan, D Trouche

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed
10.0field-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

106 citing papers in PubMed, 252 citations in OpenAlex.

  1. Article
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  6. Technologies, strategies, and cautions when deconvoluting genome-wide association signals: FTO in focus.Obesity reviews : an official journal of the International Association for the Study of Obesity · 2023
    Review
  7. Article
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  15. Vorinostat, a pan-HDAC inhibitor, abrogates productive HPV-18 DNA amplification.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Review
  17. Article
  18. Article
  19. The Temporal Regulation of S Phase Proteins During GAdvances in experimental medicine and biology · 2017
    Review
  20. Article

46 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

5 authors at 2 institutions in 1 country.

R FerreiraLaboratoire "Oncogénèse, Différenciation et Transduction du Signal," Centre National de la Recherche Scientifique Unité Propre de Recherche 9079, IFC-01, 94801 Villejuif, France.
L Magnaghi-Jaulin
P Robin
A Harel-Bellan
D Trouche
Immunology from Concept and Experiments to Translation · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transcription factor E2F plays a major role in cell cycle control in mammalian cells. E2F binding sites, which are present in the promoters of a variety of genes required for S phase, shift from a negative to a positive role in transcription at the commitment point, a crucial point in G1 that precedes the G1/S transition. Before the commitment point, E2F activity is repressed by members of the pocket proteins family. This repression is believed to be crucial for the proper control of cell growth. We have previously shown that Rb, the founding member of the pocket proteins family, represses E2F1 activity by recruiting the histone deacetylase HDAC1. Here, we show that the two other members of the pocket proteins family, p107 and p130, also are able to interact physically with HDAC1 in live cells. HDAC1 interacts with p107 and Rb through an "LXCXE"-like motif, similar to that used by viral transforming proteins to bind and inactivate pocket proteins. Indeed, we find that the viral transforming protein E1A competes with HDAC1 for p107 interaction. We also demonstrate that p107 is able to interact simultaneously with HDAC1 and E2F4, suggesting a model in which p107 recruits HDAC1 to repress E2F sites. Indeed, we demonstrate that histone deacetylase activity is involved in the p107- or p130-induced repression of E2F4. Taken together, our data suggest that all members of the E2F family are regulated in early G1 by similar complexes, containing a pocket protein and the histone deacetylase HDAC1.

Indexed as

Carrier ProteinsCell Cycle ProteinsProteinsDNA-Binding ProteinsE2F1 Transcription FactorE2F4 Transcription FactorE2F Transcription FactorsHistone DeacetylasesHumansJurkat CellsNuclear ProteinsPhosphoproteinsPhosphorylationProtein BindingRetinoblastoma-Binding Protein 1Retinoblastoma-Like Protein p107Carrier ProteinsCell Cycle ProteinsDNA-Binding ProteinsE2F1 protein, humanE2F1 Transcription FactorE2F4 protein, humanE2F4 Transcription FactorE2F Transcription FactorsHistone DeacetylasesNuclear ProteinsPhosphoproteinsProteinsRBL1 protein, humanRBL2 protein, humanRetinoblastoma-Binding Protein 1Retinoblastoma-Like Protein p107Retinoblastoma-Like Protein p130Transcription Factor DP1Transcription Factors

Identifiers

PMID9724731
PMCPMC27922
OpenAlexW1985626007

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.