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

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

Background: Nucleolar disruption is involved in cellular stress response and is sufficient for p53 activation. p53 tetramerization is crucial to exert its activity. Results: The nucleolar protein MYBBP1A enhanced p53 tetramerization by directly interacting with p53. Conclusion: p53 tetramerization by MYBBP1A is indispensable for activating p53 under nucleolar stress. Significance: This is the first report to describe the possible mechanism underlying p53 tetramerization in cells under nucleolar stress.

Original languageEnglish (US)
Pages (from-to)4928-4940
Number of pages13
JournalJournal of Biological Chemistry
Volume289
Issue number8
DOIs
StatePublished - Feb 21 2014
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Ono, W., Hayashi, Y., Yokoyama, W., Kuroda, T., Kishimoto, H., Ito, I., Kimura, K., Akaogi, K., Waku, T., & Yanagisawa, J. (2014). The nucleolar protein Myb-binding protein 1A (MYBBP1A) enhances p53 tetramerization and acetylation in response to nucleolar disruption. Journal of Biological Chemistry, 289(8), 4928-4940. https://doi.org/10.1074/jbc.M113.474049