Evidence map›Paper›PMID 12215533›Full record

ArticleMolecular and cellular biology2002

Molecular interaction and synergistic activation of a promoter by Six, Eya, and Dach proteins mediated through CREB binding protein.

Keiko Ikeda, Yoko Watanabe, Hiromi Ohto, Kiyoshi Kawakami

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

70 citing papers in PubMed, 147 citations in OpenAlex.

  1. Article
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  5. Using Xenopus to discover new candidate genes involved in BOR and other congenital hearing loss syndromes.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2024
    Review
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  20. The transcription factor Dach1 is essential for podocyte function.Journal of cellular and molecular medicine · 2018
    Article

10 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

4 authors at 1 institution in 1 country.

Keiko IkedaDepartment of Biology, Jichi Medical School, Yakushiji, Minamikawachi, Kawachi, Tochigi, 329-0498, Japan.
Yoko Watanabe
Hiromi Ohto
Kiyoshi Kawakami
Jichi Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Drosophila sine oculis, eyes absent, and dachshund are essential for compound eye formation and form a gene network with direct protein interaction and genetic regulation. The vertebrate homologues of these genes, Six, Eya, and Dach, also form a similar genetic network during muscle formation. To elucidate the molecular mechanism underlying the network among Six, Eya, and Dach, we examined the molecular interactions among the encoded proteins. Eya interacted directly with Six but never with Dach. Dach transactivated a multimerized GAL4 reporter gene by coproduction of GAL4-Eya fusion proteins. Transactivation by Eya and Dach was repressed by overexpression of VP16 or E1A but not by E1A mutation, which is defective for CREB binding protein (CBP) binding. Recruitment of CBP to the immobilized chromatin DNA template was dependent on FLAG-Dach and GAL4-Eya3. These results indicate that CBP is a mediator of the interaction between Eya and Dach. Contrary to our expectations, Dach binds to chromatin DNA by itself, not being tethered by GAL4-Eya3. Dach also binds to naked DNA with lower affinity. The conserved DD1 domain is responsible for binding to DNA. Transactivation was also observed by coproduction of GAL4-Six, Eya, and Dach, indicating that Eya and Dach synergy is relevant when Eya is tethered to DNA through Six protein. Our results demonstrated that synergy is mediated through direct interaction of Six-Eya and through the interaction of Eya-Dach with CBP and explain the molecular basis for the genetic interactions among Six, Eya, and Dach. This work provides fundamental information on the role and the mechanism of action of this gene cassette in tissue differentiation and organogenesis.

Indexed as

Saccharomyces cerevisiae Proteins3T3 CellsAnimalsCell LineChromatinCOS CellsCREB-Binding ProteinDNADNA-Binding ProteinsEye ProteinsFungal ProteinsGenes, ReporterGlutathione TransferaseHomeodomain ProteinsHumansIntracellular Signaling Peptides and ProteinsChromatinCREB-Binding ProteinCREBBP protein, humanCrebbp protein, mouseDACH1 protein, humanDach1 protein, mouseDNADNA-Binding ProteinsEYA1 protein, humanEya1 protein, mouseEya3 protein, mouseEye ProteinsFungal ProteinsGAL4 protein, S cerevisiaeGlutathione TransferaseHomeodomain ProteinsIntracellular Signaling Peptides and ProteinsNerve Tissue ProteinsNuclear ProteinsProtein Tyrosine PhosphatasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSIX1 protein, humanSix1 protein, mouseSIX2 protein, humanSIX4 protein, humanSix4 protein, mouseTrans-ActivatorsTranscription Factors

Identifiers

PMID12215533
PMCPMC134036
OpenAlexW2120147422

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.