{"title":"Protein-protein interactions regulating α-synuclein pathology.","authors":"Jiannan Wang, Lijun Dai, Sichun Chen, Zhaohui Zhang, Xin Fang, Zhentao Zhang","doi":"10.1016/j.tins.2024.01.002","DOIUrl":null,"url":null,"abstract":"<p><p>Parkinson's disease (PD) is a neurodegenerative disease characterized by the degeneration of dopaminergic neurons in the substantia nigra pars compacta (SNpc) and the formation of Lewy bodies (LBs). The main proteinaceous component of LBs is aggregated α-synuclein (α-syn). However, the mechanisms underlying α-syn aggregation are not yet fully understood. Converging lines of evidence indicate that, under certain pathological conditions, various proteins can interact with α-syn and regulate its aggregation. Understanding these protein-protein interactions is crucial for unraveling the molecular mechanisms contributing to PD pathogenesis. In this review we provide an overview of the current knowledge on protein-protein interactions that regulate α-syn aggregation. Additionally, we briefly summarize the methods used to investigate the influence of protein-protein interactions on α-syn aggregation and propagation.</p>","PeriodicalId":23325,"journal":{"name":"Trends in Neurosciences","volume":" ","pages":"209-226"},"PeriodicalIF":14.6000,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Trends in Neurosciences","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1016/j.tins.2024.01.002","RegionNum":1,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/2/13 0:00:00","PubModel":"Epub","JCR":"Q1","JCRName":"NEUROSCIENCES","Score":null,"Total":0}
引用次数: 0
Abstract
Parkinson's disease (PD) is a neurodegenerative disease characterized by the degeneration of dopaminergic neurons in the substantia nigra pars compacta (SNpc) and the formation of Lewy bodies (LBs). The main proteinaceous component of LBs is aggregated α-synuclein (α-syn). However, the mechanisms underlying α-syn aggregation are not yet fully understood. Converging lines of evidence indicate that, under certain pathological conditions, various proteins can interact with α-syn and regulate its aggregation. Understanding these protein-protein interactions is crucial for unraveling the molecular mechanisms contributing to PD pathogenesis. In this review we provide an overview of the current knowledge on protein-protein interactions that regulate α-syn aggregation. Additionally, we briefly summarize the methods used to investigate the influence of protein-protein interactions on α-syn aggregation and propagation.
帕金森病(Parkinson's disease,PD)是一种神经退行性疾病,其特征是黑质上皮(substantia nigra pars compacta,SNpc)中的多巴胺能神经元变性并形成路易体(Lewy bodies,LBs)。路易体的主要蛋白成分是聚集的α-突触核蛋白(α-syn)。然而,α-syn聚集的机制尚未完全明了。越来越多的证据表明,在某些病理条件下,各种蛋白质可与α-syn相互作用并调节其聚集。了解这些蛋白质之间的相互作用对于揭示导致帕金森病发病的分子机制至关重要。在这篇综述中,我们概述了目前有关调控α-syn聚集的蛋白-蛋白相互作用的知识。此外,我们还简要总结了用于研究蛋白-蛋白相互作用对α-syn聚集和传播的影响的方法。
期刊介绍:
For over four decades, Trends in Neurosciences (TINS) has been a prominent source of inspiring reviews and commentaries across all disciplines of neuroscience. TINS is a monthly, peer-reviewed journal, and its articles are curated by the Editor and authored by leading researchers in their respective fields. The journal communicates exciting advances in brain research, serves as a voice for the global neuroscience community, and highlights the contribution of neuroscientific research to medicine and society.