Oliveira da Silva Marina I, Liz Márcia A
Instituto de Ciências Biomédicas Abel Salazar (ICBAS), Universidade do Porto, Porto, Portugal.
Neurodegeneration Group, Instituto de Biologia Molecular e Celular (IBMC) and Nerve Regeneration Group, Instituto de Investigação e Inovação em Saúde (i3S), Universidade do Porto, Porto, Portugal.
Front Cell Dev Biol. 2020 Aug 12;8:787. doi: 10.3389/fcell.2020.00787. eCollection 2020.
Alpha-Synuclein (αSyn), a protein highly enriched in neurons where it preferentially localizes at the pre-synapse, has been in the spotlight because its intraneuronal aggregation is a central phenomenon in Parkinson's disease. However, the consequences of αSyn accumulation to neuronal function are not fully understood. Considering the crucial role of actin on synaptic function and the fact that dysregulation of this cytoskeleton component is emerging in neurodegenerative disorders, the impact of αSyn on actin is a critical point to be addressed. In this review we explore the link between αSyn and actin and its significance for physiology and pathology. We discuss the relevance of αSyn-actin interaction for synaptic function and highlight the actin-depolymerizing protein cofilin-1 as a key player on αSyn-induced actin dysfunction in Parkinson's disease.
α-突触核蛋白（αSyn）是一种在神经元中高度富集的蛋白质，它优先定位于突触前，一直备受关注，因为其在神经元内的聚集是帕金森病的核心现象。然而，αSyn积累对神经元功能的影响尚未完全了解。考虑到肌动蛋白对突触功能的关键作用，以及这种细胞骨架成分的失调在神经退行性疾病中日益凸显，αSyn对肌动蛋白的影响是一个亟待解决的关键点。在这篇综述中，我们探讨了αSyn与肌动蛋白之间的联系及其对生理和病理的意义。我们讨论了αSyn-肌动蛋白相互作用对突触功能的相关性，并强调肌动蛋白解聚蛋白cofilin-1是帕金森病中αSyn诱导的肌动蛋白功能障碍的关键因素。
