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E3 ubiquitin ligases: styles, structures and functions

E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2. E3 ubiquitin ligases play an essential role in catalyzing the ubiquitination process and transferring ubiquitin prot...

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Detalles Bibliográficos
Autores principales: Yang, Quan, Zhao, Jinyao, Chen, Dan, Wang, Yang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Singapore 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8607428/
https://www.ncbi.nlm.nih.gov/pubmed/35006464
http://dx.doi.org/10.1186/s43556-021-00043-2
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author Yang, Quan
Zhao, Jinyao
Chen, Dan
Wang, Yang
author_facet Yang, Quan
Zhao, Jinyao
Chen, Dan
Wang, Yang
author_sort Yang, Quan
collection PubMed
description E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2. E3 ubiquitin ligases play an essential role in catalyzing the ubiquitination process and transferring ubiquitin protein to attach the lysine site of targeted substrates. Importantly, ubiquitination modification is involved in almost all life activities of eukaryotes. Thus, E3 ligases might be involved in regulating various biological processes and cellular responses to stress signal associated with cancer development. Thanks to their multi-functions, E3 ligases can be a promising target of cancer therapy. A deeper understanding of the regulatory mechanisms of E3 ligases in tumorigenesis will help to find new prognostic markers and accelerate the growth of anticancer therapeutic approaches. In general, we mainly introduce the classifications of E3 ligases and their important roles in cancer progression and therapeutic functions.
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spelling pubmed-86074282021-12-01 E3 ubiquitin ligases: styles, structures and functions Yang, Quan Zhao, Jinyao Chen, Dan Wang, Yang Mol Biomed Review E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2. E3 ubiquitin ligases play an essential role in catalyzing the ubiquitination process and transferring ubiquitin protein to attach the lysine site of targeted substrates. Importantly, ubiquitination modification is involved in almost all life activities of eukaryotes. Thus, E3 ligases might be involved in regulating various biological processes and cellular responses to stress signal associated with cancer development. Thanks to their multi-functions, E3 ligases can be a promising target of cancer therapy. A deeper understanding of the regulatory mechanisms of E3 ligases in tumorigenesis will help to find new prognostic markers and accelerate the growth of anticancer therapeutic approaches. In general, we mainly introduce the classifications of E3 ligases and their important roles in cancer progression and therapeutic functions. Springer Singapore 2021-07-30 /pmc/articles/PMC8607428/ /pubmed/35006464 http://dx.doi.org/10.1186/s43556-021-00043-2 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Review
Yang, Quan
Zhao, Jinyao
Chen, Dan
Wang, Yang
E3 ubiquitin ligases: styles, structures and functions
title E3 ubiquitin ligases: styles, structures and functions
title_full E3 ubiquitin ligases: styles, structures and functions
title_fullStr E3 ubiquitin ligases: styles, structures and functions
title_full_unstemmed E3 ubiquitin ligases: styles, structures and functions
title_short E3 ubiquitin ligases: styles, structures and functions
title_sort e3 ubiquitin ligases: styles, structures and functions
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8607428/
https://www.ncbi.nlm.nih.gov/pubmed/35006464
http://dx.doi.org/10.1186/s43556-021-00043-2
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