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Phosphorylation regulates cullin-based ubiquitination in tumorigenesis
Cullin-RING ligases (CRLs) recognize and interact with substrates for ubiquitination and degradation, and can be targeted for disease treatment when the abnormal expression of substrates involves pathologic processes. Phosphorylation, either of substrates or receptors of CRLs, can alter their intera...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7893081/ https://www.ncbi.nlm.nih.gov/pubmed/33643814 http://dx.doi.org/10.1016/j.apsb.2020.09.007 |
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author | Chen, Yifan Shao, Xuejing Cao, Ji Zhu, Hong Yang, Bo He, Qiaojun Ying, Meidan |
author_facet | Chen, Yifan Shao, Xuejing Cao, Ji Zhu, Hong Yang, Bo He, Qiaojun Ying, Meidan |
author_sort | Chen, Yifan |
collection | PubMed |
description | Cullin-RING ligases (CRLs) recognize and interact with substrates for ubiquitination and degradation, and can be targeted for disease treatment when the abnormal expression of substrates involves pathologic processes. Phosphorylation, either of substrates or receptors of CRLs, can alter their interaction. Phosphorylation-dependent ubiquitination and proteasome degradation influence various cellular processes and can contribute to the occurrence of various diseases, most often tumorigenesis. These processes have the potential to be used for tumor intervention through the regulation of the activities of related kinases, along with the regulation of the stability of specific oncoproteins and tumor suppressors. This review describes the mechanisms and biological functions of crosstalk between phosphorylation and ubiquitination, and most importantly its influence on tumorigenesis, to provide new directions and strategies for tumor therapy. |
format | Online Article Text |
id | pubmed-7893081 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-78930812021-02-25 Phosphorylation regulates cullin-based ubiquitination in tumorigenesis Chen, Yifan Shao, Xuejing Cao, Ji Zhu, Hong Yang, Bo He, Qiaojun Ying, Meidan Acta Pharm Sin B Review Cullin-RING ligases (CRLs) recognize and interact with substrates for ubiquitination and degradation, and can be targeted for disease treatment when the abnormal expression of substrates involves pathologic processes. Phosphorylation, either of substrates or receptors of CRLs, can alter their interaction. Phosphorylation-dependent ubiquitination and proteasome degradation influence various cellular processes and can contribute to the occurrence of various diseases, most often tumorigenesis. These processes have the potential to be used for tumor intervention through the regulation of the activities of related kinases, along with the regulation of the stability of specific oncoproteins and tumor suppressors. This review describes the mechanisms and biological functions of crosstalk between phosphorylation and ubiquitination, and most importantly its influence on tumorigenesis, to provide new directions and strategies for tumor therapy. Elsevier 2021-02 2020-09-19 /pmc/articles/PMC7893081/ /pubmed/33643814 http://dx.doi.org/10.1016/j.apsb.2020.09.007 Text en © 2021 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences. Production and hosting by Elsevier B.V. http://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 | Review Chen, Yifan Shao, Xuejing Cao, Ji Zhu, Hong Yang, Bo He, Qiaojun Ying, Meidan Phosphorylation regulates cullin-based ubiquitination in tumorigenesis |
title | Phosphorylation regulates cullin-based ubiquitination in tumorigenesis |
title_full | Phosphorylation regulates cullin-based ubiquitination in tumorigenesis |
title_fullStr | Phosphorylation regulates cullin-based ubiquitination in tumorigenesis |
title_full_unstemmed | Phosphorylation regulates cullin-based ubiquitination in tumorigenesis |
title_short | Phosphorylation regulates cullin-based ubiquitination in tumorigenesis |
title_sort | phosphorylation regulates cullin-based ubiquitination in tumorigenesis |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7893081/ https://www.ncbi.nlm.nih.gov/pubmed/33643814 http://dx.doi.org/10.1016/j.apsb.2020.09.007 |
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