Evidence map›Paper›PMID 29232376›Full record

ArticlePloS one2017

Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes.

Gizem Caliskan, Ikbal C Baris, Ferhan Ayaydin, Melanie J Dobson, Muge Senarisoy, Imre M Boros, Zeki Topcu, Sevil Zencir

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. CK2-mediated phosphorylation of Che-1/AATF is required for its pro-proliferative activity.Journal of experimental & clinical cancer research : CR · 2021
    Article
  4. Article
  5. Article
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

8 authors at 5 institutions in 3 countries.

Gizem CaliskanDepartment of Pharmaceutical Biotechnology, Faculty of Pharmacy, Ege University, Izmir, Turkey.
Ikbal C BarisDepartment of Medical Biology, Faculty of Medicine, Pamukkale University, Denizli, Turkey.
Ferhan AyaydinCellular Imaging Laboratory, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
Melanie J DobsonDepartment of Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS, Canada.
Muge SenarisoyDepartment of Pharmaceutical Biotechnology, Faculty of Pharmacy, Ege University, Izmir, Turkey.
Imre M BorosInstitute of Biochemistry, Hungarian Academy of Sciences, Szeged, Hungary.
Zeki TopcuDepartment of Pharmaceutical Biotechnology, Faculty of Pharmacy, Ege University, Izmir, Turkey.
Sevil ZencirDepartment of Medical Biology, Faculty of Medicine, Pamukkale University, Denizli, Turkey.ORCID http://orcid.org/0000-0002-9937-5712
Ege University · TRPamukkale University · TRDalhousie University · CAHungarian Academy of Sciences · HUInstitute of Biochemistry · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

General Control Non-derepressible 5 (GCN5) and Alteration/Deficiency in Activation 2 and 3 proteins (ADA2 and ADA3, respectively) are subunits of the Histone AcetylTransferase (HAT) module of SAGA- and ATAC-type co-activators. We previously reported four new interacting partners of human ADA3 identified by screening a human fetal brain cDNA library using yeast two hybrid technology. One of these partners was Apoptosis-Antagonizing Transcription Factor (AATF), also known as Che-1, an RNA polymerase II-binding protein with a number of roles in different cellular processes including regulation of transcription, cell proliferation, cell cycle control, DNA damage responses and apoptosis. Che-1/AATF is a potential therapeutic target for cancer treatments. In this study, we aimed to identify whether besides ADA3, other components of the HAT modules of SAGA and ATAC complexes, human ADA2 and GCN5 also interact with Che-1/AATF. Co-immunoprecipitation and co-localization experiments were used to demonstrate association of AATF both with two ADA2 isoforms, ADA2A and ADA2B and with GCN5 proteins in human cells and yeast two-hybrid assays to delineate domains in the ADA2 and GCN5 proteins required for these interactions. These findings provide new insights into the pathways regulated by ADA-containing protein complexes.

Indexed as

AcetyltransferasesAdaptor Proteins, Signal TransducingDNA-Binding ProteinsHistone AcetyltransferasesHumansp300-CBP-Associated Factorp300-CBP Transcription FactorsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscriptional ActivationTranscription FactorsAcetyltransferasesAdaptor Proteins, Signal TransducingDNA-Binding ProteinsHistone Acetyltransferasesp300-CBP-Associated Factorp300-CBP Transcription FactorsSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeSgf29 protein, humanTADA2A protein, humanTADA2B protein, humanTrans-ActivatorsTranscription Factors

Identifiers

PMID29232376
PMCPMC5726650
OpenAlexW2773201251

What OpenQuestion holds

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LicenceCC BY
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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.