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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...

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Autores principales: Chen, Yifan, Shao, Xuejing, Cao, Ji, Zhu, Hong, Yang, Bo, He, Qiaojun, Ying, Meidan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2021
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.
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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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