Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy
Abstract Intracellular vesicle trafficking is the fundamental process to maintain the homeostasis of membrane-enclosed organelles in eukaryotic cells. These organelles transport cargo from the donor membrane to the target membrane through the cargo containing vesicles. Vesicle trafficking pathway in...
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Springer
2022-09-01
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Online Access: | https://doi.org/10.1186/s43556-022-00090-3 |
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author | Lele Cui Hao Li Yufeng Xi Qianli Hu Huimin Liu Jiaqi Fan Yijuan Xiang Xing Zhang Weiwei Shui Ying Lai |
author_facet | Lele Cui Hao Li Yufeng Xi Qianli Hu Huimin Liu Jiaqi Fan Yijuan Xiang Xing Zhang Weiwei Shui Ying Lai |
author_sort | Lele Cui |
collection | DOAJ |
description | Abstract Intracellular vesicle trafficking is the fundamental process to maintain the homeostasis of membrane-enclosed organelles in eukaryotic cells. These organelles transport cargo from the donor membrane to the target membrane through the cargo containing vesicles. Vesicle trafficking pathway includes vesicle formation from the donor membrane, vesicle transport, and vesicle fusion with the target membrane. Coat protein mediated vesicle formation is a delicate membrane budding process for cargo molecules selection and package into vesicle carriers. Vesicle transport is a dynamic and specific process for the cargo containing vesicles translocation from the donor membrane to the target membrane. This process requires a group of conserved proteins such as Rab GTPases, motor adaptors, and motor proteins to ensure vesicle transport along cytoskeletal track. Soluble N-ethyl-maleimide-sensitive factor (NSF) attachment protein receptors (SNARE)-mediated vesicle fusion is the final process for vesicle unloading the cargo molecules at the target membrane. To ensure vesicle fusion occurring at a defined position and time pattern in eukaryotic cell, multiple fusogenic proteins, such as synaptotagmin (Syt), complexin (Cpx), Munc13, Munc18 and other tethering factors, cooperate together to precisely regulate the process of vesicle fusion. Dysfunctions of the fusogenic proteins in SNARE-mediated vesicle fusion are closely related to many diseases. Recent studies have suggested that stimulated membrane fusion can be manipulated pharmacologically via disruption the interface between the SNARE complex and Ca2+ sensor protein. Here, we summarize recent insights into the molecular mechanisms of vesicle trafficking, and implications for the development of new therapeutics based on the manipulation of vesicle fusion. |
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institution | Directory Open Access Journal |
issn | 2662-8651 |
language | English |
last_indexed | 2024-04-12T20:14:13Z |
publishDate | 2022-09-01 |
publisher | Springer |
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series | Molecular Biomedicine |
spelling | doaj.art-d0ede02abc5740aa859fa16a90ff5db52022-12-22T03:18:11ZengSpringerMolecular Biomedicine2662-86512022-09-013113310.1186/s43556-022-00090-3Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapyLele Cui0Hao Li1Yufeng Xi2Qianli Hu3Huimin Liu4Jiaqi Fan5Yijuan Xiang6Xing Zhang7Weiwei Shui8Ying Lai9National Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityNational Clinical Research Center for Geriatrics, State Key Laboratory of Biotherapy and Collaborative Innovation Center of Biotherapy, West China Hospital, Sichuan UniversityAbstract Intracellular vesicle trafficking is the fundamental process to maintain the homeostasis of membrane-enclosed organelles in eukaryotic cells. These organelles transport cargo from the donor membrane to the target membrane through the cargo containing vesicles. Vesicle trafficking pathway includes vesicle formation from the donor membrane, vesicle transport, and vesicle fusion with the target membrane. Coat protein mediated vesicle formation is a delicate membrane budding process for cargo molecules selection and package into vesicle carriers. Vesicle transport is a dynamic and specific process for the cargo containing vesicles translocation from the donor membrane to the target membrane. This process requires a group of conserved proteins such as Rab GTPases, motor adaptors, and motor proteins to ensure vesicle transport along cytoskeletal track. Soluble N-ethyl-maleimide-sensitive factor (NSF) attachment protein receptors (SNARE)-mediated vesicle fusion is the final process for vesicle unloading the cargo molecules at the target membrane. To ensure vesicle fusion occurring at a defined position and time pattern in eukaryotic cell, multiple fusogenic proteins, such as synaptotagmin (Syt), complexin (Cpx), Munc13, Munc18 and other tethering factors, cooperate together to precisely regulate the process of vesicle fusion. Dysfunctions of the fusogenic proteins in SNARE-mediated vesicle fusion are closely related to many diseases. Recent studies have suggested that stimulated membrane fusion can be manipulated pharmacologically via disruption the interface between the SNARE complex and Ca2+ sensor protein. Here, we summarize recent insights into the molecular mechanisms of vesicle trafficking, and implications for the development of new therapeutics based on the manipulation of vesicle fusion.https://doi.org/10.1186/s43556-022-00090-3Vesicle formationVesicle transportVesicle fusionFusogenic proteinsDisease therapy |
spellingShingle | Lele Cui Hao Li Yufeng Xi Qianli Hu Huimin Liu Jiaqi Fan Yijuan Xiang Xing Zhang Weiwei Shui Ying Lai Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy Molecular Biomedicine Vesicle formation Vesicle transport Vesicle fusion Fusogenic proteins Disease therapy |
title | Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy |
title_full | Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy |
title_fullStr | Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy |
title_full_unstemmed | Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy |
title_short | Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy |
title_sort | vesicle trafficking and vesicle fusion mechanisms biological functions and their implications for potential disease therapy |
topic | Vesicle formation Vesicle transport Vesicle fusion Fusogenic proteins Disease therapy |
url | https://doi.org/10.1186/s43556-022-00090-3 |
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