Evidence map›Paper›PMID 12371907›Full record

ArticleThe Biochemical journal2003

p300/cAMP-response-element-binding-protein ('CREB')-binding protein (CBP) modulates co-operation between myocyte enhancer factor 2A (MEF2A) and thyroid hormone receptor-retinoid X receptor.

Antonio De Luca, Anna Severino, Paola De Paolis, Giuliano Cottone, Luca De Luca, Maria De Falco, Antonio Porcellini, Massimo Volpe, Gianluigi Condorelli

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

16 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. ACAA2 is a ligand-dependent coactivator for thyroid hormone receptor β1.Biochemical and biophysical research communications · 2021
    Article
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  7. Article
  8. Review
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  10. Review
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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

9 authors at 4 institutions in 1 country.

Antonio De LucaDepartment of Experimental Medicine and Pathology, IRCCS, Neuromed, Rome, Italy. antonio.deluca@unina2.it
Anna Severino
Paola De Paolis
Giuliano Cottone
Luca De Luca
Maria De Falco
Antonio Porcellini
Massimo Volpe
Gianluigi Condorelli
Istituto Neurologico Mediterraneo · ITFederico II University Hospital · ITUniversity of Campania "Luigi Vanvitelli" · ITUniversity of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thyroid hormone receptors (TRs) and members of the myocyte enhancer factor 2 (MEF2) family are involved in the regulation of muscle-specific gene expression during myogenesis. Physical interaction between these two factors is required to synergistically activate gene transcription. p300/cAMP-response-element-binding-protein ('CREB')-binding protein (CBP) interacting with transcription factors is able to increase their activity on target gene promoters. We investigated the role of p300 in regulating the TR-MEF2A complex. To this end, we mapped the regions of these proteins involved in physical interactions and we evaluated the expression of a chloramphenicol acetyltransferase (CAT) reporter gene in U2OS cells under control of the alpha-myosin heavy chain promoter containing the thyroid hormone response element (TRE). Our results suggested a role of p300/CBP in mediating the transactivation effects of the TR-retenoid X receptor (RxR)-MEF2A complex. Our findings showed that the same C-terminal portion of p300 binds the N-terminal domains of both TR and MEF2A, and our in vivo studies demonstrated that TR, MEF2A and p300 form a ternary complex. Moreover, by the use of CAT assays, we demonstrated that adenovirus E1A inhibits activation of transcription by TR-RxR-MEF2A-p300 but not by TR-RxR-MEF2A. Our data suggested that p300 can bind and modulate the activity of TR-RxR-MEF2A at TRE. In addition, it is speculated that p300 might modulate the activity of the TR-RxR-MEF2A complex by recruiting a hypothetical endogenous inhibitor which may act like adenovirus E1A.

Indexed as

AnimalsCells, CulturedChloramphenicol O-AcetyltransferaseChromatinCOS CellsDNA-Binding ProteinsElectrophoretic Mobility Shift AssayHumansMADS Domain ProteinsMEF2 Transcription FactorsMyogenic Regulatory FactorsNuclear ProteinsReceptors, Retinoic AcidReceptors, Thyroid HormoneRetinoid X ReceptorsTrans-ActivatorsChloramphenicol O-AcetyltransferaseChromatinDNA-Binding ProteinsMADS Domain ProteinsMEF2A protein, humanMEF2 Transcription FactorsMyogenic Regulatory FactorsNuclear ProteinsReceptors, Retinoic AcidReceptors, Thyroid HormoneRetinoid X ReceptorsTrans-ActivatorsTranscription Factors

Identifiers

PMID12371907
PMCPMC1223100
OpenAlexW2005405898

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.