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NUSAP1 potentiates chemoresistance in glioblastoma through its SAP domain to stabilize ATR
NUSAP1, which is a microtubule-associated protein involved in mitosis, plays essential roles in diverse biological processes, especially in cancer biology. In this study, NUSAP1 was found to be overexpressed in GBM tissues in a grade-dependent manner compared with normal brain tissues. NUSAP1 was al...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7174393/ https://www.ncbi.nlm.nih.gov/pubmed/32317623 http://dx.doi.org/10.1038/s41392-020-0137-7 |
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author | Zhao, Yuzu He, Jiang Li, Yongsen Lv, Shengqing Cui, Hongjuan |
author_facet | Zhao, Yuzu He, Jiang Li, Yongsen Lv, Shengqing Cui, Hongjuan |
author_sort | Zhao, Yuzu |
collection | PubMed |
description | NUSAP1, which is a microtubule-associated protein involved in mitosis, plays essential roles in diverse biological processes, especially in cancer biology. In this study, NUSAP1 was found to be overexpressed in GBM tissues in a grade-dependent manner compared with normal brain tissues. NUSAP1 was also highly expressed in GBM patients, dead patients, and GBM cells. In addition, NUSAP1 was found to participate in cell proliferation, apoptosis, and DNA damage in GBM cells. Ataxia telangiectasia and Rad3-related protein (ATR) are a primary sensor of DNA damage, and ATR is also a promising target in cancer therapy. Here, we found that NUSAP1 positively regulated the expression of ATR. Mechanistically, NUSAP1 suppressed the ubiquitin-dependent proteolysis of ATR. The SAP (SAF-A/B, Acinus, and PIAS) domain is a common motif of many SUMO (small ubiquitin-like modifier) E3 ligases, and this domain is involved in substrate recognition and ligase activity. This study further demonstrated that the SAP domain of NUSAP1 promoted the sumoylation of ATR, and thereby antagonized the ubiquitination of ATR. These results suggest that NUSAP1 stabilizes ATR by sumoylation. Moreover, NUSAP1 potentiated chemotherapeutic resistance to temozolomide (TMZ) and doxorubicin (DOX) through its SAP domain. Overall, this study indicates that NUSAP1 is a promising therapeutic target in GBM. |
format | Online Article Text |
id | pubmed-7174393 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-71743932020-04-29 NUSAP1 potentiates chemoresistance in glioblastoma through its SAP domain to stabilize ATR Zhao, Yuzu He, Jiang Li, Yongsen Lv, Shengqing Cui, Hongjuan Signal Transduct Target Ther Article NUSAP1, which is a microtubule-associated protein involved in mitosis, plays essential roles in diverse biological processes, especially in cancer biology. In this study, NUSAP1 was found to be overexpressed in GBM tissues in a grade-dependent manner compared with normal brain tissues. NUSAP1 was also highly expressed in GBM patients, dead patients, and GBM cells. In addition, NUSAP1 was found to participate in cell proliferation, apoptosis, and DNA damage in GBM cells. Ataxia telangiectasia and Rad3-related protein (ATR) are a primary sensor of DNA damage, and ATR is also a promising target in cancer therapy. Here, we found that NUSAP1 positively regulated the expression of ATR. Mechanistically, NUSAP1 suppressed the ubiquitin-dependent proteolysis of ATR. The SAP (SAF-A/B, Acinus, and PIAS) domain is a common motif of many SUMO (small ubiquitin-like modifier) E3 ligases, and this domain is involved in substrate recognition and ligase activity. This study further demonstrated that the SAP domain of NUSAP1 promoted the sumoylation of ATR, and thereby antagonized the ubiquitination of ATR. These results suggest that NUSAP1 stabilizes ATR by sumoylation. Moreover, NUSAP1 potentiated chemotherapeutic resistance to temozolomide (TMZ) and doxorubicin (DOX) through its SAP domain. Overall, this study indicates that NUSAP1 is a promising therapeutic target in GBM. Nature Publishing Group UK 2020-04-22 /pmc/articles/PMC7174393/ /pubmed/32317623 http://dx.doi.org/10.1038/s41392-020-0137-7 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Zhao, Yuzu He, Jiang Li, Yongsen Lv, Shengqing Cui, Hongjuan NUSAP1 potentiates chemoresistance in glioblastoma through its SAP domain to stabilize ATR |
title | NUSAP1 potentiates chemoresistance in glioblastoma through its SAP domain to stabilize ATR |
title_full | NUSAP1 potentiates chemoresistance in glioblastoma through its SAP domain to stabilize ATR |
title_fullStr | NUSAP1 potentiates chemoresistance in glioblastoma through its SAP domain to stabilize ATR |
title_full_unstemmed | NUSAP1 potentiates chemoresistance in glioblastoma through its SAP domain to stabilize ATR |
title_short | NUSAP1 potentiates chemoresistance in glioblastoma through its SAP domain to stabilize ATR |
title_sort | nusap1 potentiates chemoresistance in glioblastoma through its sap domain to stabilize atr |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7174393/ https://www.ncbi.nlm.nih.gov/pubmed/32317623 http://dx.doi.org/10.1038/s41392-020-0137-7 |
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