Evidence map›Paper›PMID 15735663›Full record

ArticleOncogene2005

A functional interaction between ATF7 and TAF12 that is modulated by TAF4.

Pierre-Jacques Hamard, Rozenn Dalbies-Tran, Charlotte Hauss, Irwin Davidson, Claude Kedinger, Bruno Chatton

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Role of ATF7-TAF12 interactions in the vitamin D response hypersensitivity of osteoclast precursors in Paget's disease.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2013
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  7. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  13. Pathobiology of Paget's Disease of Bone.Journal of bone metabolism · 2014
    Review
  14. Article
  15. Article
  16. Distinct modes of gene regulation by a cell-specific transcriptional activator.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
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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

6 authors at 4 institutions in 1 country.

Pierre-Jacques HamardEcole Supérieure de Biotechnologie de Strasbourg, Université Louis Pasteur, Parc d'innovation, UMR7100 CNRS-ULP, Bd. Sebastien Brant-BP10413, 67412 Strasbourg, Illkirch Cedex, France.
Rozenn Dalbies-Tran
Charlotte Hauss
Irwin Davidson
Claude Kedinger
Bruno Chatton
Centre National de la Recherche Scientifique · FRÉcole Normale Supérieure - PSL · FRÉcole Supérieure de Biotechnologie de Strasbourg · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ATF7 proteins, which are members of the cyclic AMP responsive binding protein (CREB)/activating transcription factor (ATF) family of transcription factors, display quite versatile properties: they can interact with the adenovirus E1a oncoprotein, mediating part of its transcriptional activity; they heterodimerize with the Jun, Fos or related transcription factors, likely modulating their DNA-binding specificity; they also recruit to the promoter a stress-induced protein kinase (JNK2). In the present study, we investigate the functional relationships of ATF7 with hsTAF12 (formerly hsTAF(II)20/15), which has originally been identified as a component of the general transcription factor TFIID. We show that overexpression of hsTAF12 potentiates ATF7-induced transcriptional activation through direct interaction with ATF7, suggesting that TAF12 is a functional partner of ATF7. In support of this conclusion, chromatin immunoprecipitation experiments confirm the interaction of ATF7 with TAF12 on an ATF7-responsive promoter, in the absence of any artificial overexpression of both proteins. We also show that the TAF12-dependent transcriptional activation is competitively inhibited by TAF4. Although both TAF12 isoforms (TAF12-1 and -2, formerly TAF(II)20 and TAF(II)15) interact with the ATF7 activation region through their histone-fold domain, only the largest, hsTAF12-1, mediates transcriptional activation through its N-terminal region.

Indexed as

Gene Expression RegulationActivating Transcription FactorsAmino Acid SequenceAnimalsCell LineChromatinDNA-Binding ProteinsHumansImmunoprecipitationInsectaLeucine ZippersMolecular Sequence DataOligonucleotide Array Sequence AnalysisReverse Transcriptase Polymerase Chain ReactionTATA-Binding Protein Associated FactorsTranscription FactorsActivating Transcription FactorsATF7 protein, humanChromatinDNA-Binding ProteinsTAF12 protein, humanTAF4 protein, humanTATA-Binding Protein Associated FactorsTranscription FactorsTranscription Factor TFIID

Identifiers

PMID15735663
OpenAlexW2029581772

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.