Portrait of WWP1: the current state in human cancer
WWP1, a member of the C2-WW-HECT E3 ligase family, is an E3 ubiquitin-protein ligase containing WW domains. This enzyme plays a critical role in regulating diverse cellular processes. Its expression is modulated by various factors and non-coding RNAs, resulting in ubiquitination that affects substra...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2025-01-01
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| Series: | Frontiers in Cell and Developmental Biology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fcell.2024.1516613/full |
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| author | Jiaming Lei Jun Chen Wenwen Yu Qing Wu Shuang Jing Yuanguang Tang Li Lin Meichun Hu |
| author_facet | Jiaming Lei Jun Chen Wenwen Yu Qing Wu Shuang Jing Yuanguang Tang Li Lin Meichun Hu |
| author_sort | Jiaming Lei |
| collection | DOAJ |
| description | WWP1, a member of the C2-WW-HECT E3 ligase family, is an E3 ubiquitin-protein ligase containing WW domains. This enzyme plays a critical role in regulating diverse cellular processes. Its expression is modulated by various factors and non-coding RNAs, resulting in ubiquitination that affects substrate protein degradation. WWP1 demonstrates a dual function, acting predominantly as an oncogene in tumors but occasionally as a tumor suppressor. This review summarizes WWP1’s biological roles, therapeutic potential in oncology, upstream regulatory factors, and downstream substrates. It aims to promote research on WWP1’s antitumor effects, improve understanding of its role in tumorigenesis, and support the development of targeted therapies. |
| format | Article |
| id | doaj-art-05e6701c8c2446e59a5b3adf792eaba3 |
| institution | Kabale University |
| issn | 2296-634X |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cell and Developmental Biology |
| spelling | doaj-art-05e6701c8c2446e59a5b3adf792eaba32025-01-30T06:23:00ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2025-01-011210.3389/fcell.2024.15166131516613Portrait of WWP1: the current state in human cancerJiaming Lei0Jun Chen1Wenwen Yu2Qing Wu3Shuang Jing4Yuanguang Tang5Li Lin6Meichun Hu7Key Laboratory of Environmental Related Diseases and One Health, School of Basic Medical Sciences, Xianning Medical College, Hubei University of Science and Technology, Xianning, Hubei, ChinaThe Central Hospital of Ezhou, Affiliated Hospital of Hubei University of Science and Technology, Ezhou, Hubei, ChinaKey Laboratory of Environmental Related Diseases and One Health, School of Basic Medical Sciences, Xianning Medical College, Hubei University of Science and Technology, Xianning, Hubei, ChinaState Key Laboratory of Genetic Resources and Evolution, Key Laboratory of Healthy Aging Research of Yunnan Province, Kunming Key Laboratory of Healthy Aging Study, KIZ/CUHK Joint Laboratory of Bioresources and Molecular Research in Common Diseases, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan, ChinaKey Laboratory of Environmental Related Diseases and One Health, School of Basic Medical Sciences, Xianning Medical College, Hubei University of Science and Technology, Xianning, Hubei, ChinaKey Laboratory of Environmental Related Diseases and One Health, School of Basic Medical Sciences, Xianning Medical College, Hubei University of Science and Technology, Xianning, Hubei, ChinaKey Laboratory of Environmental Related Diseases and One Health, School of Basic Medical Sciences, Xianning Medical College, Hubei University of Science and Technology, Xianning, Hubei, ChinaKey Laboratory of Environmental Related Diseases and One Health, School of Basic Medical Sciences, Xianning Medical College, Hubei University of Science and Technology, Xianning, Hubei, ChinaWWP1, a member of the C2-WW-HECT E3 ligase family, is an E3 ubiquitin-protein ligase containing WW domains. This enzyme plays a critical role in regulating diverse cellular processes. Its expression is modulated by various factors and non-coding RNAs, resulting in ubiquitination that affects substrate protein degradation. WWP1 demonstrates a dual function, acting predominantly as an oncogene in tumors but occasionally as a tumor suppressor. This review summarizes WWP1’s biological roles, therapeutic potential in oncology, upstream regulatory factors, and downstream substrates. It aims to promote research on WWP1’s antitumor effects, improve understanding of its role in tumorigenesis, and support the development of targeted therapies.https://www.frontiersin.org/articles/10.3389/fcell.2024.1516613/fullWWP1human cancerupstream factordownstream substratetargeted therapy |
| spellingShingle | Jiaming Lei Jun Chen Wenwen Yu Qing Wu Shuang Jing Yuanguang Tang Li Lin Meichun Hu Portrait of WWP1: the current state in human cancer Frontiers in Cell and Developmental Biology WWP1 human cancer upstream factor downstream substrate targeted therapy |
| title | Portrait of WWP1: the current state in human cancer |
| title_full | Portrait of WWP1: the current state in human cancer |
| title_fullStr | Portrait of WWP1: the current state in human cancer |
| title_full_unstemmed | Portrait of WWP1: the current state in human cancer |
| title_short | Portrait of WWP1: the current state in human cancer |
| title_sort | portrait of wwp1 the current state in human cancer |
| topic | WWP1 human cancer upstream factor downstream substrate targeted therapy |
| url | https://www.frontiersin.org/articles/10.3389/fcell.2024.1516613/full |
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