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Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation

The mammalian Sirt1 deacetylase is generally thought to be a nuclear protein, but some pilot studies have suggested that Sirt1 may also be involved in orchestrating nucleolar functions. Here, we show that nucleolar stress response is a ubiquitous cellular reaction that can be induced by different ty...

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Detalles Bibliográficos
Autores principales: Bi, Xiaolei, Ye, Qing, Li, Daoyuan, Peng, Qisheng, Wang, Zhe, Wu, Xiao, Zhang, Yun, Zhang, Qunye, Jiang, Fan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6413664/
https://www.ncbi.nlm.nih.gov/pubmed/30623565
http://dx.doi.org/10.1111/acel.12900
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author Bi, Xiaolei
Ye, Qing
Li, Daoyuan
Peng, Qisheng
Wang, Zhe
Wu, Xiao
Zhang, Yun
Zhang, Qunye
Jiang, Fan
author_facet Bi, Xiaolei
Ye, Qing
Li, Daoyuan
Peng, Qisheng
Wang, Zhe
Wu, Xiao
Zhang, Yun
Zhang, Qunye
Jiang, Fan
author_sort Bi, Xiaolei
collection PubMed
description The mammalian Sirt1 deacetylase is generally thought to be a nuclear protein, but some pilot studies have suggested that Sirt1 may also be involved in orchestrating nucleolar functions. Here, we show that nucleolar stress response is a ubiquitous cellular reaction that can be induced by different types of stress conditions, and Sirt1 is an endogenous suppressor of nucleolar stress response. Using stable isotope labeling by amino acids in cell culture approach, we have identified a physical interaction of between Sirt1 and the nucleolar protein nucleophosmin, and this protein–protein interaction appears to be necessary for Sirt1 inhibition on nucleolar stress, whereas the deacetylase activity of Sirt1 is not strictly required. Based on the reported prerequisite role of nucleolar stress response in stress‐induced p53 protein accumulation, we have also provided evidence suggesting that Sirt1‐mediated inhibition on nucleolar stress response may represent a novel mechanism by which Sirt1 can modulate intracellular p53 accumulation independent of lysine deacetylation. This process may represent an alternative mechanism by which Sirt1 regulates functions of the p53 pathway.
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spelling pubmed-64136642019-04-01 Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation Bi, Xiaolei Ye, Qing Li, Daoyuan Peng, Qisheng Wang, Zhe Wu, Xiao Zhang, Yun Zhang, Qunye Jiang, Fan Aging Cell Original Papers The mammalian Sirt1 deacetylase is generally thought to be a nuclear protein, but some pilot studies have suggested that Sirt1 may also be involved in orchestrating nucleolar functions. Here, we show that nucleolar stress response is a ubiquitous cellular reaction that can be induced by different types of stress conditions, and Sirt1 is an endogenous suppressor of nucleolar stress response. Using stable isotope labeling by amino acids in cell culture approach, we have identified a physical interaction of between Sirt1 and the nucleolar protein nucleophosmin, and this protein–protein interaction appears to be necessary for Sirt1 inhibition on nucleolar stress, whereas the deacetylase activity of Sirt1 is not strictly required. Based on the reported prerequisite role of nucleolar stress response in stress‐induced p53 protein accumulation, we have also provided evidence suggesting that Sirt1‐mediated inhibition on nucleolar stress response may represent a novel mechanism by which Sirt1 can modulate intracellular p53 accumulation independent of lysine deacetylation. This process may represent an alternative mechanism by which Sirt1 regulates functions of the p53 pathway. John Wiley and Sons Inc. 2019-01-08 2019-04 /pmc/articles/PMC6413664/ /pubmed/30623565 http://dx.doi.org/10.1111/acel.12900 Text en © 2019 The Authors. Aging Cell published by the Anatomical Society and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Papers
Bi, Xiaolei
Ye, Qing
Li, Daoyuan
Peng, Qisheng
Wang, Zhe
Wu, Xiao
Zhang, Yun
Zhang, Qunye
Jiang, Fan
Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation
title Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation
title_full Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation
title_fullStr Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation
title_full_unstemmed Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation
title_short Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation
title_sort inhibition of nucleolar stress response by sirt1: a potential mechanism of acetylation‐independent regulation of p53 accumulation
topic Original Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6413664/
https://www.ncbi.nlm.nih.gov/pubmed/30623565
http://dx.doi.org/10.1111/acel.12900
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