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A novel role of proteasomal β1 subunit in tumorigenesis

p27(Kip1) is a key cell-cycle regulator whose level is primarily regulated by the ubiquitin–proteasome degradation pathway. Its β1 subunit is one of seven β subunits that form the β-ring of the 20S proteasome, which is responsible for degradation of ubiquitinated proteins. We report here that the β1...

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Autores principales: Yuan, Fuqiang, Ma, Yana, You, Pan, Lin, Wenbo, Lu, Haojie, Yu, Yinhua, Wang, Xiaomin, Jiang, Jie, Yang, Pengyuan, Ma, Qilin, Tao, Tao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3712487/
https://www.ncbi.nlm.nih.gov/pubmed/23725357
http://dx.doi.org/10.1042/BSR20130013
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author Yuan, Fuqiang
Ma, Yana
You, Pan
Lin, Wenbo
Lu, Haojie
Yu, Yinhua
Wang, Xiaomin
Jiang, Jie
Yang, Pengyuan
Ma, Qilin
Tao, Tao
author_facet Yuan, Fuqiang
Ma, Yana
You, Pan
Lin, Wenbo
Lu, Haojie
Yu, Yinhua
Wang, Xiaomin
Jiang, Jie
Yang, Pengyuan
Ma, Qilin
Tao, Tao
author_sort Yuan, Fuqiang
collection PubMed
description p27(Kip1) is a key cell-cycle regulator whose level is primarily regulated by the ubiquitin–proteasome degradation pathway. Its β1 subunit is one of seven β subunits that form the β-ring of the 20S proteasome, which is responsible for degradation of ubiquitinated proteins. We report here that the β1 subunit is up-regulated in oesophageal cancer tissues and some ovarian cancer cell lines. It promotes cell growth and migration, as well as colony formation. β1 binds and degrades p27(Kip1)directly. Interestingly, the lack of phosphorylation at Ser(158) of the β1 subunit promotes degradation of p27(Kip1). We therefore propose that the β1 subunit plays a novel role in tumorigenesis by degrading p27(Kip1).
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spelling pubmed-37124872013-07-23 A novel role of proteasomal β1 subunit in tumorigenesis Yuan, Fuqiang Ma, Yana You, Pan Lin, Wenbo Lu, Haojie Yu, Yinhua Wang, Xiaomin Jiang, Jie Yang, Pengyuan Ma, Qilin Tao, Tao Biosci Rep Original Paper p27(Kip1) is a key cell-cycle regulator whose level is primarily regulated by the ubiquitin–proteasome degradation pathway. Its β1 subunit is one of seven β subunits that form the β-ring of the 20S proteasome, which is responsible for degradation of ubiquitinated proteins. We report here that the β1 subunit is up-regulated in oesophageal cancer tissues and some ovarian cancer cell lines. It promotes cell growth and migration, as well as colony formation. β1 binds and degrades p27(Kip1)directly. Interestingly, the lack of phosphorylation at Ser(158) of the β1 subunit promotes degradation of p27(Kip1). We therefore propose that the β1 subunit plays a novel role in tumorigenesis by degrading p27(Kip1). Portland Press Ltd. 2013-07-16 /pmc/articles/PMC3712487/ /pubmed/23725357 http://dx.doi.org/10.1042/BSR20130013 Text en © 2013 The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Licence (CC-BY)(http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Paper
Yuan, Fuqiang
Ma, Yana
You, Pan
Lin, Wenbo
Lu, Haojie
Yu, Yinhua
Wang, Xiaomin
Jiang, Jie
Yang, Pengyuan
Ma, Qilin
Tao, Tao
A novel role of proteasomal β1 subunit in tumorigenesis
title A novel role of proteasomal β1 subunit in tumorigenesis
title_full A novel role of proteasomal β1 subunit in tumorigenesis
title_fullStr A novel role of proteasomal β1 subunit in tumorigenesis
title_full_unstemmed A novel role of proteasomal β1 subunit in tumorigenesis
title_short A novel role of proteasomal β1 subunit in tumorigenesis
title_sort novel role of proteasomal β1 subunit in tumorigenesis
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3712487/
https://www.ncbi.nlm.nih.gov/pubmed/23725357
http://dx.doi.org/10.1042/BSR20130013
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