Increasing evidence suggests that α-synuclein is a common pathogenic molecule in several neurodegenerative diseases, particularly in Parkinson's disease. To understand α-synuclein pathology, we investigated molecules that interact with α-synuclein in human and rat brains and identified tubulin as an α-synuclein binding/associated protein. Tubulin co-localized with α-synuclein in Lewy bodies and other α-synuclein-positive pathological structures. Tubulin initiated and promoted α-synuclein fibril formation under physiological conditions in vitro. These findings suggest that an interaction between tubulin and α-synuclein might accelerate α-synuclein aggregation in diseased brains, leading to the formation of Lewy bodies.
CITATION STYLE
Alim, M. A., Hossain, M. S., Arima, K., Takeda, K., Izumiyama, Y., Nakamura, M., … Uéda, K. (2002). Tubulin seeds α-synuclein fibril formation. Journal of Biological Chemistry, 277(3), 2112–2117. https://doi.org/10.1074/jbc.M102981200
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