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USP39-mediated deubiquitination of Cyclin B1 promotes tumor cell proliferation and glioma progression
BACKGROUND: The elevated Cyclin B1 expression contributes to various tumorigenesis and poor prognosis. Cyclin B1 expression could be regulated by ubiquitination and deubiquitination. However, the mechanism of how Cyclin B1 is deubiquitinated and its roles in human glioma remain unclear. METHODS: Co-...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Neoplasia Press
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10302533/ https://www.ncbi.nlm.nih.gov/pubmed/37302347 http://dx.doi.org/10.1016/j.tranon.2023.101713 |
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author | Xiao, Yue Chen, Xinyi Hu, Weiwei Ma, Wenjing Di, Qianqian Tang, Haimei Zhao, Xibao Huang, Guodong Chen, Weilin |
author_facet | Xiao, Yue Chen, Xinyi Hu, Weiwei Ma, Wenjing Di, Qianqian Tang, Haimei Zhao, Xibao Huang, Guodong Chen, Weilin |
author_sort | Xiao, Yue |
collection | PubMed |
description | BACKGROUND: The elevated Cyclin B1 expression contributes to various tumorigenesis and poor prognosis. Cyclin B1 expression could be regulated by ubiquitination and deubiquitination. However, the mechanism of how Cyclin B1 is deubiquitinated and its roles in human glioma remain unclear. METHODS: Co-immunoprecipitation and other assays were performed to detect the interacting of Cyclin B1 and USP39. A series of in vitro and in vivo experiments were performed to investigate the effect of USP39 on the tumorigenicity of tumor cells. RESULTS: USP39 interacts with Cyclin B1 and stabilizes its expression by deubiquitinating Cyclin B1. Notably, USP39 cleaves the K29-linked polyubiquitin chain on Cyclin B1 at Lys242. Additionally, overexpression of Cyclin B1 rescues the arrested cell cycle at G2/M transition and the suppressed proliferation of glioma cells caused by USP39 knockdown in vitro. Furthermore, USP39 promotes the growth of glioma xenograft in subcutaneous and in situ of nude mice. Finally, in human tumor specimens, the expression levels of USP39 and Cyclin B1 are positively relevant. CONCLUSION: Our data support the evidence that USP39 acts a novel deubiquitinating enzyme of Cyclin B1 and promoted tumor cell proliferation at least in part through Cyclin B1 stabilization, represents a promising therapeutic strategy for tumor patients. |
format | Online Article Text |
id | pubmed-10302533 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Neoplasia Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-103025332023-06-29 USP39-mediated deubiquitination of Cyclin B1 promotes tumor cell proliferation and glioma progression Xiao, Yue Chen, Xinyi Hu, Weiwei Ma, Wenjing Di, Qianqian Tang, Haimei Zhao, Xibao Huang, Guodong Chen, Weilin Transl Oncol Original Research BACKGROUND: The elevated Cyclin B1 expression contributes to various tumorigenesis and poor prognosis. Cyclin B1 expression could be regulated by ubiquitination and deubiquitination. However, the mechanism of how Cyclin B1 is deubiquitinated and its roles in human glioma remain unclear. METHODS: Co-immunoprecipitation and other assays were performed to detect the interacting of Cyclin B1 and USP39. A series of in vitro and in vivo experiments were performed to investigate the effect of USP39 on the tumorigenicity of tumor cells. RESULTS: USP39 interacts with Cyclin B1 and stabilizes its expression by deubiquitinating Cyclin B1. Notably, USP39 cleaves the K29-linked polyubiquitin chain on Cyclin B1 at Lys242. Additionally, overexpression of Cyclin B1 rescues the arrested cell cycle at G2/M transition and the suppressed proliferation of glioma cells caused by USP39 knockdown in vitro. Furthermore, USP39 promotes the growth of glioma xenograft in subcutaneous and in situ of nude mice. Finally, in human tumor specimens, the expression levels of USP39 and Cyclin B1 are positively relevant. CONCLUSION: Our data support the evidence that USP39 acts a novel deubiquitinating enzyme of Cyclin B1 and promoted tumor cell proliferation at least in part through Cyclin B1 stabilization, represents a promising therapeutic strategy for tumor patients. Neoplasia Press 2023-06-09 /pmc/articles/PMC10302533/ /pubmed/37302347 http://dx.doi.org/10.1016/j.tranon.2023.101713 Text en © 2023 The Authors. Published by Elsevier Inc. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Original Research Xiao, Yue Chen, Xinyi Hu, Weiwei Ma, Wenjing Di, Qianqian Tang, Haimei Zhao, Xibao Huang, Guodong Chen, Weilin USP39-mediated deubiquitination of Cyclin B1 promotes tumor cell proliferation and glioma progression |
title | USP39-mediated deubiquitination of Cyclin B1 promotes tumor cell proliferation and glioma progression |
title_full | USP39-mediated deubiquitination of Cyclin B1 promotes tumor cell proliferation and glioma progression |
title_fullStr | USP39-mediated deubiquitination of Cyclin B1 promotes tumor cell proliferation and glioma progression |
title_full_unstemmed | USP39-mediated deubiquitination of Cyclin B1 promotes tumor cell proliferation and glioma progression |
title_short | USP39-mediated deubiquitination of Cyclin B1 promotes tumor cell proliferation and glioma progression |
title_sort | usp39-mediated deubiquitination of cyclin b1 promotes tumor cell proliferation and glioma progression |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10302533/ https://www.ncbi.nlm.nih.gov/pubmed/37302347 http://dx.doi.org/10.1016/j.tranon.2023.101713 |
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