Evidence map›Paper›PMID 16432238›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

The methyl-CpG binding protein MBD1 is required for PML-RARalpha function.

Raffaella Villa, Lluis Morey, Veronica A Raker, Marcus Buschbeck, Arantxa Gutierrez, Francesca De Santis, Massimo Corsaro, Florencio Varas, Daniela Bossi, Saverio Minucci and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
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  10. DNA Methylation and Adult Neurogenesis.Brain plasticity (Amsterdam, Netherlands) · 2017
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. An epigenetic regulator: methyl-CpG-binding domain protein 1 (MBD1).International journal of molecular sciences · 2015
    Review
  17. Histone deacetylase inhibitors and cell death.Cellular and molecular life sciences : CMLS · 2014
    Review
  18. Article
  19. 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

12 authors at 3 institutions in 2 countries.

Raffaella VillaCentre de Regulacio Genomica, Universitat Pompeu Fabra, Passeig Maritim 37-49, 08003 Barcelona, Spain.
Lluis Morey
Veronica A Raker
Marcus Buschbeck
Arantxa Gutierrez
Francesca De Santis
Massimo Corsaro
Florencio Varas
Daniela Bossi
Saverio Minucci
Pier Giuseppe Pelicci
Luciano Di Croce
European Institute of Oncology · ITPompeu Fabra University · ESInstitució Catalana de Recerca i Estudis Avançats · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PML-RARalpha induces a block of hematopoietic differentiation and acute promyelocytic leukemia. This block is based on its capacity to inactivate target genes by recruiting histone deacetylase (HDAC) and DNA methyltransferase activities. Here we report that MBD1, a member of a conserved family of proteins able to bind methylated DNA, cooperates with PML-RARalpha in transcriptional repression and cellular transformation. PML-RARalpha recruits MBD1 to its target promoter through an HDAC3-mediated mechanism. Binding of HDAC3 and MBD1 is not confined to the promoter region but instead is spread over the locus. Knock-down of HDAC3 expression by RNA interference in acute promyelocytic leukemia cells alleviates PML-RAR-induced promoter silencing. We further demonstrate that retroviral expression of dominant-negative mutants of MBD1 in hematopoietic precursors compromises the ability of PML-RARalpha to block their differentiation and thus restored cell differentiation. Our results demonstrate that PML-RARalpha functions by recruiting an HDAC3-MBD1 complex that contributes to the establishment and maintenance of the silenced chromatin state.

Indexed as

Blotting, WesternCell DifferentiationCell LineCell Line, TumorCell Transformation, NeoplasticChromatinChromatin ImmunoprecipitationDNA-Binding ProteinsDNA, ComplementaryEpigenesis, GeneticGenes, DominantGene SilencingGenetic VectorsHeLa CellsHematopoietic Stem CellsHistone Deacetylase 3ChromatinDNA-Binding ProteinsDNA, ComplementaryHistone Deacetylase 3Histone DeacetylasesLuciferasesMBD1 protein, humanNeoplasm ProteinsOligonucleotidesOncogene Proteins, Fusionpromyelocytic leukemia-retinoic acid receptor alpha fusion oncoproteinTranscription Factors

Identifiers

PMID16432238
PMCPMC1360559
OpenAlexW2144967170

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.