E3 ubiquitin ligase SYVN1 as a promising therapeutic target for diverse human diseases
Numerous studies conducted in recent years indicate that mammalian E3 ubiquitin ligases serve as key regulators in the maintenance of cellular homeostasis by targeting the ubiquitination of substrate proteins and activating downstream signaling pathways. SYVN1, an E3 ubiquitin ligase, is characteriz...
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Elsevier
2025-02-01
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| Series: | Pharmacological Research |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S1043661825000283 |
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| author | Li Zhu Yong-Ping Liu Yuan-Wang Bo-Xuan Sun Yu-Ting Huang Ji-Kai Zhao Jian-Feng Liu Li-Ming Yu Hui-Shan Wang |
| author_facet | Li Zhu Yong-Ping Liu Yuan-Wang Bo-Xuan Sun Yu-Ting Huang Ji-Kai Zhao Jian-Feng Liu Li-Ming Yu Hui-Shan Wang |
| author_sort | Li Zhu |
| collection | DOAJ |
| description | Numerous studies conducted in recent years indicate that mammalian E3 ubiquitin ligases serve as key regulators in the maintenance of cellular homeostasis by targeting the ubiquitination of substrate proteins and activating downstream signaling pathways. SYVN1, an E3 ubiquitin ligase, is characterized by its significant functions in regulating various biological processes, including molecular mechanisms related to gene expression, signaling pathways, and cell death, among others. Consequently, SYVN1 plays a crucial role in both normal human physiology and the pathogenesis of various diseases, such as oncogenesis, cardiovascular disorders, immune regulation, skeletal anomalies, and neurological diseases. This review synthesizes recent findings regarding the physiological and pathophysiological roles of SYVN1, offering new insights into potential strategies for the prevention and treatment of human diseases, as well as suggesting avenues for future drug development. In this Review, we summarize the latest findings regarding the physiological and pathophysiological roles of SYVN1, elucidating the mechanisms by which SYVN1 can regulate the progression of various diseases in humans. These important findings provide new avenues for further investigation of SYVN1 protein, new insights into potential strategies to prevent and treat human diseases, and new directions for future drug development. |
| format | Article |
| id | doaj-art-31a6cd925cf74ea7836aef16e4f82695 |
| institution | Kabale University |
| issn | 1096-1186 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Pharmacological Research |
| spelling | doaj-art-31a6cd925cf74ea7836aef16e4f826952025-02-08T04:59:49ZengElsevierPharmacological Research1096-11862025-02-01212107603E3 ubiquitin ligase SYVN1 as a promising therapeutic target for diverse human diseasesLi Zhu0Yong-Ping Liu1 Yuan-Wang2Bo-Xuan Sun3Yu-Ting Huang4Ji-Kai Zhao5Jian-Feng Liu6Li-Ming Yu7Hui-Shan Wang8Graduate School of Dalian Medical University, Dalian, Liaoning 116000, China; State Key Laboratory of Frigid Zone Cardiovascular Disease, Department of Cardiovascular Surgery, General Hospital of Northern Theater Command, Shenyang, Liaoning 110016, ChinaDepartment of Pediatrics, Shengjing Hospital of China Medical University, Shenyang, Liaoning 110004, ChinaGraduate School of Dalian Medical University, Dalian, Liaoning 116000, China; State Key Laboratory of Frigid Zone Cardiovascular Disease, Department of Cardiovascular Surgery, General Hospital of Northern Theater Command, Shenyang, Liaoning 110016, ChinaState Key Laboratory of Frigid Zone Cardiovascular Disease, Department of Cardiovascular Surgery, General Hospital of Northern Theater Command, Shenyang, Liaoning 110016, ChinaState Key Laboratory of Frigid Zone Cardiovascular Disease, Department of Cardiovascular Surgery, General Hospital of Northern Theater Command, Shenyang, Liaoning 110016, ChinaState Key Laboratory of Frigid Zone Cardiovascular Disease, Department of Cardiovascular Surgery, General Hospital of Northern Theater Command, Shenyang, Liaoning 110016, ChinaFirst School of Clinical Medicine, Shenyang Medical College, Shenyang, Liaoning 110034, ChinaState Key Laboratory of Frigid Zone Cardiovascular Disease, Department of Cardiovascular Surgery, General Hospital of Northern Theater Command, Shenyang, Liaoning 110016, China; Correspondence to: State Key Laboratory of Frigid Zone Cardiovascular Disease, Department of Cardiovascular Surgery, General Hospital of Northern Theater Command, 83 Wenhua Road, Shenyang City 110016, China.State Key Laboratory of Frigid Zone Cardiovascular Disease, Department of Cardiovascular Surgery, General Hospital of Northern Theater Command, Shenyang, Liaoning 110016, China; Correspondence to: State Key Laboratory of Frigid Zone Cardiovascular Disease, Department of Cardiovascular Surgery, General Hospital of Northern Theater Command, 83 Wenhua Road, Shenyang City 110016, China.Numerous studies conducted in recent years indicate that mammalian E3 ubiquitin ligases serve as key regulators in the maintenance of cellular homeostasis by targeting the ubiquitination of substrate proteins and activating downstream signaling pathways. SYVN1, an E3 ubiquitin ligase, is characterized by its significant functions in regulating various biological processes, including molecular mechanisms related to gene expression, signaling pathways, and cell death, among others. Consequently, SYVN1 plays a crucial role in both normal human physiology and the pathogenesis of various diseases, such as oncogenesis, cardiovascular disorders, immune regulation, skeletal anomalies, and neurological diseases. This review synthesizes recent findings regarding the physiological and pathophysiological roles of SYVN1, offering new insights into potential strategies for the prevention and treatment of human diseases, as well as suggesting avenues for future drug development. In this Review, we summarize the latest findings regarding the physiological and pathophysiological roles of SYVN1, elucidating the mechanisms by which SYVN1 can regulate the progression of various diseases in humans. These important findings provide new avenues for further investigation of SYVN1 protein, new insights into potential strategies to prevent and treat human diseases, and new directions for future drug development.http://www.sciencedirect.com/science/article/pii/S1043661825000283SYVN1Cancer diseaseE3 ubiquitin ligase |
| spellingShingle | Li Zhu Yong-Ping Liu Yuan-Wang Bo-Xuan Sun Yu-Ting Huang Ji-Kai Zhao Jian-Feng Liu Li-Ming Yu Hui-Shan Wang E3 ubiquitin ligase SYVN1 as a promising therapeutic target for diverse human diseases Pharmacological Research SYVN1 Cancer disease E3 ubiquitin ligase |
| title | E3 ubiquitin ligase SYVN1 as a promising therapeutic target for diverse human diseases |
| title_full | E3 ubiquitin ligase SYVN1 as a promising therapeutic target for diverse human diseases |
| title_fullStr | E3 ubiquitin ligase SYVN1 as a promising therapeutic target for diverse human diseases |
| title_full_unstemmed | E3 ubiquitin ligase SYVN1 as a promising therapeutic target for diverse human diseases |
| title_short | E3 ubiquitin ligase SYVN1 as a promising therapeutic target for diverse human diseases |
| title_sort | e3 ubiquitin ligase syvn1 as a promising therapeutic target for diverse human diseases |
| topic | SYVN1 Cancer disease E3 ubiquitin ligase |
| url | http://www.sciencedirect.com/science/article/pii/S1043661825000283 |
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