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Tubulin seeds alpha-synuclein fibril formation.
Authors:Muhammad Abdul Alim  Mosammat Shahanara Hossain  Kunimasa Arima  Kazuya Takeda  Yoko Izumiyama  Minako Nakamura  Hiroyuki Kaji  Tomotaka Shinoda  Shinichi Hisanaga  Kenji Ueda
Institution:Department of Neural Plasticity, Tokyo Institute of Psychiatry, Setagaya-ku, Tokyo 156-8585, Japan.
Abstract:Increasing evidence suggests that alpha-synuclein is a common pathogenic molecule in several neurodegenerative diseases, particularly in Parkinson's disease. To understand alpha-synuclein pathology, we investigated molecules that interact with alpha-synuclein in human and rat brains and identified tubulin as an alpha-synuclein binding/associated protein. Tubulin co-localized with alpha-synuclein in Lewy bodies and other alpha-synuclein-positive pathological structures. Tubulin initiated and promoted alpha-synuclein fibril formation under physiological conditions in vitro. These findings suggest that an interaction between tubulin and alpha-synuclein might accelerate alpha-synuclein aggregation in diseased brains, leading to the formation of Lewy bodies.
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