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...
Guardado en:
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 |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/4c56454ffebd47ce98598764f25ff35c |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
The enzyme activity of mitochondrial trifunctional protein is not altered by lysine acetylation or lysine succinylation.
por: Yuxun Zhang, et al.
Publicado: (2021) -
Reader domain specificity and lysine demethylase-4 family function
por: Zhangli Su, et al.
Publicado: (2016) -
Global analysis of lysine acetylation in soybean leaves
por: Geng Li, et al.
Publicado: (2021) -
Lysine acetylation regulates the interaction between proteins and membranes
por: Alan K. Okada, et al.
Publicado: (2021) -
Ancient Regulatory Role of Lysine Acetylation in Central Metabolism
por: Ernesto S. Nakayasu, et al.
Publicado: (2017)