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

31 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",

year = "2014",

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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.

UR - https://www.scopus.com/pages/publications/84896703015

UR - https://www.scopus.com/pages/publications/84896703015#tab=citedBy

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DO - 10.1074/jbc.M113.474049

M3 - Article

C2 - 24375404

AN - SCOPUS:84896703015

SN - 0021-9258

VL - 289

SP - 4928

EP - 4940

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 8

ER -

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

Abstract

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