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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Main Authors: Lele Cui, Hao Li, Yufeng Xi, Qianli Hu, Huimin Liu, Jiaqi Fan, Yijuan Xiang, Xing Zhang, Weiwei Shui, Ying Lai
Format: Article
Language:English
Published: Springer 2022-09-01
Series:Molecular Biomedicine
Subjects:
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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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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