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tau蛋白与α-突触核蛋白的液-液相分离:神经病理学重叠的新途径。

Liquid-liquid phase separation of tau and α-synuclein: A new pathway of overlapping neuropathologies.

作者信息

Rodríguez Leandro Cruz, Foressi Nahuel N, Celej M Soledad

机构信息

Departamento de Química Biológica Ranwel Caputto, Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC, CONICET), Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Haya de la Torre y Medina Allende, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.

Departamento de Química Biológica Ranwel Caputto, Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC, CONICET), Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Haya de la Torre y Medina Allende, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.

出版信息

Biochem Biophys Res Commun. 2024 Dec 31;741:151053. doi: 10.1016/j.bbrc.2024.151053. Epub 2024 Nov 23.

Abstract

Liquid-liquid phase separation (LLPS) is a critical phenomenon that leads to the formation of liquid-like membrane-less organelles within cells. Advances in our understanding of condensates reveal their significant roles in biology and highlight how their dysregulation may contribute to disease. Recent evidence indicates that the high protein concentration in coacervates may lead to abnormal protein aggregation associated with several neurodegenerative diseases. The presence of condensates containing multiple amyloidogenic proteins may play a role in the co-deposition and comorbidity seen in neurodegeneration. This review first provides a brief overview of the physicochemical bases and molecular determinants of LLPS. It then summarizes our understanding of Tau and α-synuclein (AS) phase separation, key proteins in Alzheimer's and Parkinson's diseases. By integrating recent findings on complex Tau and AS coacervation, this article offers a fresh perspective on how LLPS may contribute to the pathological overlap in neurodegenerative disorders and provide a novel therapeutic target to mitigate or prevent such conditions.

摘要

液-液相分离(LLPS)是一种关键现象,它导致细胞内形成类液无膜细胞器。我们对凝聚物认识的进展揭示了它们在生物学中的重要作用,并突出了其失调可能如何导致疾病。最近的证据表明,凝聚物中高蛋白质浓度可能导致与几种神经退行性疾病相关的异常蛋白质聚集。含有多种淀粉样蛋白生成蛋白的凝聚物的存在可能在神经退行性变中所见的共沉积和共病中起作用。本综述首先简要概述了LLPS的物理化学基础和分子决定因素。然后总结了我们对Tau蛋白和α-突触核蛋白(AS)相分离的理解,它们是阿尔茨海默病和帕金森病中的关键蛋白。通过整合关于复杂的Tau蛋白和AS凝聚的最新发现,本文就LLPS如何导致神经退行性疾病中的病理重叠提供了新的视角,并提供了一个减轻或预防此类病症的新治疗靶点。

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