Linking Alpha-Synuclein to the Actin Cytoskeleton: Consequences to Neuronal Function

被引:22
作者
Oliveira da Silva, Marina I. [1 ,2 ,3 ]
Liz, Marcia A. [2 ,3 ]
机构
[1] Univ Porto, Inst Ciencias Biomed Abel Salazar ICBAS, Porto, Portugal
[2] Univ Porto, Neurodegenerat Grp, Inst Biol Mol & Celular IBMC, Porto, Portugal
[3] Univ Porto, Nerve Regenerat Grp, Inst Invest & Inovacao Saude i3S, Porto, Portugal
关键词
alpha-Synuclein; Parkinson's disease; actin cytoskeleton; actin-binding proteins; cofilin-1; IN-VIVO; ALZHEIMERS-DISEASE; DROSOPHILA MODEL; ARP2/3; COMPLEX; KNOCKOUT MICE; PROTEINS; COFILIN; MICROTUBULES; PHOSPHORYLATION; INHIBITION;
D O I
10.3389/fcell.2020.00787
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Alpha-Synuclein (alpha Syn), 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 alpha Syn 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 alpha Syn on actin is a critical point to be addressed. In this review we explore the link between alpha Syn and actin and its significance for physiology and pathology. We discuss the relevance of alpha Syn-actin interaction for synaptic function and highlight the actin-depolymerizing protein cofilin-1 as a key player on alpha Syn-induced actin dysfunction in Parkinson's disease.
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页数:8
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