PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth

Acetylation of p53 is critical for its transcriptional activity and its tumour suppressive function. Here, the authors show that PBRM1 is a reader protein for p53′s C-terminal domain acetylation on lysine 382 through its bromodomain 4 and that mutations in this domain leads to compromised tumour sup...

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Autores principales: Weijia Cai, Liya Su, Lili Liao, Zongzhi Z. Liu, Lauren Langbein, Essel Dulaimi, Joseph R. Testa, Robert G. Uzzo, Zhijiu Zhong, Wei Jiang, Qin Yan, Qing Zhang, Haifeng Yang
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/4c56454ffebd47ce98598764f25ff35c
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spelling oai:doaj.org-article:4c56454ffebd47ce98598764f25ff35c2021-12-02T14:39:02ZPBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth10.1038/s41467-019-13608-12041-1723https://doaj.org/article/4c56454ffebd47ce98598764f25ff35c2019-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13608-1https://doaj.org/toc/2041-1723Acetylation of p53 is critical for its transcriptional activity and its tumour suppressive function. Here, the authors show that PBRM1 is a reader protein for p53′s C-terminal domain acetylation on lysine 382 through its bromodomain 4 and that mutations in this domain leads to compromised tumour suppressive function and renal tumour growth.Weijia CaiLiya SuLili LiaoZongzhi Z. LiuLauren LangbeinEssel DulaimiJoseph R. TestaRobert G. UzzoZhijiu ZhongWei JiangQin YanQing ZhangHaifeng YangNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Weijia Cai
Liya Su
Lili Liao
Zongzhi Z. Liu
Lauren Langbein
Essel Dulaimi
Joseph R. Testa
Robert G. Uzzo
Zhijiu Zhong
Wei Jiang
Qin Yan
Qing Zhang
Haifeng Yang
PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth
description Acetylation of p53 is critical for its transcriptional activity and its tumour suppressive function. Here, the authors show that PBRM1 is a reader protein for p53′s C-terminal domain acetylation on lysine 382 through its bromodomain 4 and that mutations in this domain leads to compromised tumour suppressive function and renal tumour growth.
format article
author Weijia Cai
Liya Su
Lili Liao
Zongzhi Z. Liu
Lauren Langbein
Essel Dulaimi
Joseph R. Testa
Robert G. Uzzo
Zhijiu Zhong
Wei Jiang
Qin Yan
Qing Zhang
Haifeng Yang
author_facet Weijia Cai
Liya Su
Lili Liao
Zongzhi Z. Liu
Lauren Langbein
Essel Dulaimi
Joseph R. Testa
Robert G. Uzzo
Zhijiu Zhong
Wei Jiang
Qin Yan
Qing Zhang
Haifeng Yang
author_sort Weijia Cai
title PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth
title_short PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth
title_full PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth
title_fullStr PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth
title_full_unstemmed PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth
title_sort pbrm1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/4c56454ffebd47ce98598764f25ff35c
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