Evidence map›Paper›PMID 30952900›Full record

ArticleScientific reports2019

The human HOXA9 protein uses paralog-specific residues of the homeodomain to interact with TALE-class cofactors.

Amélie Dard, Yunlong Jia, Jonathan Reboulet, Françoise Bleicher, Catherine Lavau, Samir Merabet

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. HOXA9 Regulome and Pharmacological Interventions in Leukemia.Advances in experimental medicine and biology · 2024
    Review
  6. Article
  7. Hox genes in development and beyond.Development (Cambridge, England) · 2023
    Article
  8. Article
  9. Diversification and Functional Evolution of HOX Proteins.Frontiers in cell and developmental biology · 2022
    Review
  10. Review
  11. Review
  12. Review
  13. A Synthetic CPP33-ConjugatedBiomolecules · 2020
    Article
  14. Review
  15. Review
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 2 institutions in 2 countries.

Amélie DardInstitut de Génomique Fonctionnelle de Lyon, Université de Lyon, Université Lyon 1, CNRS, Ecole Normale Supérieure de Lyon, 46 allée d'Italie 69364, Lyon cedex, 07, France.
Yunlong JiaInstitut de Génomique Fonctionnelle de Lyon, Université de Lyon, Université Lyon 1, CNRS, Ecole Normale Supérieure de Lyon, 46 allée d'Italie 69364, Lyon cedex, 07, France.ORCID http://orcid.org/0000-0001-7111-0520
Jonathan RebouletInstitut de Génomique Fonctionnelle de Lyon, Université de Lyon, Université Lyon 1, CNRS, Ecole Normale Supérieure de Lyon, 46 allée d'Italie 69364, Lyon cedex, 07, France.
Françoise BleicherInstitut de Génomique Fonctionnelle de Lyon, Université de Lyon, Université Lyon 1, CNRS, Ecole Normale Supérieure de Lyon, 46 allée d'Italie 69364, Lyon cedex, 07, France.
Catherine LavauNeurosurgery, Duke University Medical Center, Research Drive, LSRC building, Room C-243, Box 91001, Durham, NC, 27710, USA.
Samir MerabetInstitut de Génomique Fonctionnelle de Lyon, Université de Lyon, Université Lyon 1, CNRS, Ecole Normale Supérieure de Lyon, 46 allée d'Italie 69364, Lyon cedex, 07, France. samir.merabet@ens-lyon.fr.
Université Claude Bernard Lyon 1 · FRDuke Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HOX proteins interact with PBX and MEIS cofactors, which belong to the TALE-class of homeodomain (HD)-containing transcription factors. Although the formation of HOX-PBX complexes depends on a unique conserved HOX motif called hexapeptide (HX), the additional presence of MEIS induces a remodeling of the interaction, leading to a global dispensability of the HX motif for trimeric complex formation in the large majority of HOX proteins. In addition, it was shown that the anterior HOXB3 and central HOXA7 and HOXC8 proteins could use different alternative TALE interaction motifs, with or without the HX motif, depending on the DNA-binding site and cell context. Here we dissected the molecular interaction properties of the human posterior HOXA9 protein with its TALE cofactors, PBX1 and MEIS1. Analysis was performed on different DNA-binding sites in vitro and by doing Bimolecular Fluorescence Complementation (BiFC) in different cell lines. Notably, we observed that the HOXA9-TALE interaction relies consistently on the redundant activity of the HX motif and two paralog-specific residues of the HOXA9 HD. Together with previous work, our results show that HOX proteins interact with their generic TALE cofactors through various modalities, ranging from unique and context-independent to versatile and context-dependent TALE binding interfaces.

Indexed as

Binding SitesCell LineCell Line, TumorDNADNA-Binding ProteinsHeLa CellsHomeodomain ProteinsHumansMCF-7 CellsNeoplasm ProteinsProtein BindingTranscription FactorsDNADNA-Binding Proteinshomeobox protein HOXA9Homeodomain ProteinsNeoplasm ProteinsTranscription Factors

Identifiers

PMID30952900
PMCPMC6450960
OpenAlexW2927181208

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.