The behavior of α-synuclein in neurons

• Published in: Movement disorders Vol. 25; no. S1; pp. S21 - S26
• Main Authors: Fortin, Doris L., Nemani, Venu M., Nakamura, Ken, Edwards, Robert H.
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 2010; Wiley
• Subjects: alpha-Synuclein - genetics; alpha-Synuclein - metabolism; Biological and medical sciences; Calcium - metabolism; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases; exocytosis; Humans; Medical sciences; mobility; Mutation - genetics; Neurology; neuron; Neurons - metabolism; Parkinson Disease - genetics; Parkinson Disease - pathology; Parkinson's disease; synaptic vesicle; α-synuclein; Nervous system diseases; Parkinson's disease; Parkinson disease; Mobility; Synaptic vesicle; Cerebral disorder; Neuron; Central nervous system disease; Degenerative disease; exocytosis; Behavior; α-synuclein; Extrapyramidal syndrome
• ISSN: 0885-3185; 1531-8257
• DOI: 10.1002/mds.22722

Despite considerable evidence linking α‐synuclein with membranes in vitro, it has proven difficult to demonstrate membrane association of the protein in vivo. α‐Synuclein localizes to the nerve terminal, but biochemical experiments have not revealed a tight association with membranes. To address the dynamics of the protein in live cells, we have used photobleaching and found that α‐synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of α‐synuclein, causing its dispersion from the synapse. In addition to the presumed role of α‐synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease. © 2010 Movement Disorder Society