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

doi:10.1074/jbc.M113.474049

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 journal › Article › peer-review

29 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 language	English (US)
Pages (from-to)	4928-4940
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	289
Issue number	8
DOIs	https://doi.org/10.1074/jbc.M113.474049
State	Published - Feb 21 2014
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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

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.",

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

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day = "21",

doi = "10.1074/jbc.M113.474049",

language = "English (US)",

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journal = "Journal of Biological Chemistry",

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TY - JOUR

T1 - The nucleolar protein Myb-binding protein 1A (MYBBP1A) enhances p53 tetramerization and acetylation in response to nucleolar disruption

AU - Ono, Wakana

AU - Hayashi, Yuki

AU - Yokoyama, Wataru

AU - Kuroda, Takao

AU - Kishimoto, Hiroyuki

AU - Ito, Ichiaki

AU - Kimura, Keiji

AU - Akaogi, Kensuke

AU - Waku, Tsuyoshi

AU - Yanagisawa, Junn

PY - 2014/2/21

Y1 - 2014/2/21

N2 - 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.

AB - 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.

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

Abstract

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