Destruction of synaptic vesicles by alpha-synuclein
The neurodegenerative disorder Parkinson's disease is becoming progressively more widespread as our population ages, resulting in thousands of deaths globally each year. The cause of this disease is poorly understood, however onset is associated with an accumulation of the protein, a-synuclein, in the brain. In its monomeric form, a-synuclein is a small (<10 nm), intrinsically disordered soluble protein that is involved in neurotransmitter release. However, it has the propensity to aggregate into large, rigid structures known as fibrils that have a characteristic beta-sheet structure and are insoluble in water. a-synuclein is known to bind to synaptic vesicles and modulate vesicle recycling and homeostasis. In a-synuclein overexpression models synaptic vesicles become clustered, rendering them unavailable for release. As such, release of the neurotransmitter dopamine contained within these vesicles is also reduced, as well as the number of vesicles themselves. A current gap in our understanding of the role of a-synuclein in disease is whether its accumulation in cells directly leads to the degradation of synaptic vesicles, and if so, what is the mechanism.
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The recommended format for citing this dataset in a research publication is in the following format:
Thomas M. McCoy; ARMSTRONG Alexander; CUBITT Robert; KAMINSKI Gabi; LEMMEL Hartmut; ROUTH Alexander and Amberley D. Stephens. (2020). Destruction of synaptic vesicles by alpha-synuclein. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-999
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