Impacts of increased α-synuclein on clathrin-mediated endocytosis at synapses : implications for neurodegenerative diseases

© The Author(s), 2018. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Neural Regeneration Research 13 (2018): 647-648, doi:10.4103/1673-5374.230289.Parkinson's disease (PD) is a neurodegenerative disease that impacts the lives of millions of people worldwide. A pathological hallmark of PD, as well as dementia with Lewy bodies (DLB) and several Alzheimer's disease variants, is the appearance of intracellular inclusions called Lewy bodies, which contain high levels of aggregated α-synuclein. α-Synuclein is a presynaptic protein that normally associates with synaptic vesicle membranes and regulates synaptic vesicle trafficking under physiological conditions (Calo et al., 2016). However, in familial PD, multiplication and several point mutations in the α-synuclein gene (SNCA) ultimately lead to toxic aggregation of the α-synuclein protein and subsequent degeneration of dopaminergic neurons in the substantia nigra, although other brain areas are also affected (Schulz-Schaeffer, 2010).This research was supported by a grant from National Institutes of Health (NINDS/NIA R01NS078165 to JRM), research funds from the Marine Biological Laboratory (to JRM), and a research grant from Horizon 2020 Grant No. InCure EU Joint Programme-JPND (to LB)