Evidence map›Paper›PMID 24375404›Full record

ArticleThe Journal of biological chemistry2014

The nucleolar protein Myb-binding protein 1A (MYBBP1A) enhances p53 tetramerization and acetylation in response to nucleolar disruption.

Wakana Ono, Yuki Hayashi, Wataru Yokoyama, Takao Kuroda, Hiroyuki Kishimoto, Ichiaki Ito, Keiji Kimura, Kensuke Akaogi, Tsuyoshi Waku, Junn Yanagisawa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 21% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

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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

10 authors at 3 institutions in 1 country.

Wakana OnoFrom the Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba Science City, Ibaraki 305-8577, Japan.
Yuki Hayashi
Wataru Yokoyama
Takao Kuroda
Hiroyuki Kishimoto
Ichiaki Ito
Keiji Kimura
Kensuke Akaogi
Tsuyoshi Waku
Junn Yanagisawa
University of Tsukuba · JPDoshisha University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tetramerization of p53 is crucial to exert its biological activity, and nucleolar disruption is sufficient to activate p53. We previously demonstrated that nucleolar stress induces translocation of the nucleolar protein MYBBP1A from the nucleolus to the nucleoplasm and enhances p53 activity. However, whether and how MYBBP1A regulates p53 tetramerization in response to nucleolar stress remain unclear. In this study, we demonstrated that MYBBP1A enhances p53 tetramerization, followed by acetylation under nucleolar stress. We found that MYBBP1A has two regions that directly bind to lysine residues of the p53 C-terminal regulatory domain. MYBBP1A formed a self-assembled complex that provided a molecular platform for p53 tetramerization and enhanced p300-mediated acetylation of the p53 tetramer. Moreover, our results show that MYBBP1A functions to enhance p53 tetramerization that is necessary for p53 activation, followed by cell death with actinomycin D treatment. Thus, we suggest that MYBBP1A plays a pivotal role in the cellular stress response.

Indexed as

Protein MultimerizationAcetylationBinding SitesCell Line, TumorCell NucleolusDNA-Binding ProteinsE1A-Associated p300 ProteinHumansModels, BiologicalNuclear ProteinsNucleocytoplasmic Transport ProteinsPromoter Regions, GeneticProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsRNA-Binding ProteinsDNA-Binding ProteinsE1A-Associated p300 ProteinEP300 protein, humanMYBBP1A protein, humanNuclear ProteinsNucleocytoplasmic Transport ProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsTranscription FactorsTumor Suppressor Protein p53Cell DeathNucleolusp300p53Post-translational ModificationStress Response

Identifiers

PMID24375404
PMCPMC3931054
OpenAlexW1989435094

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.