Impairment of microtubule system increases alpha-synuclein aggregation and toxicity |
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Authors: | Kim Myunghye Jung Wonsuk Lee In-Hwan Bhak Ghibom Paik Seung R Hahn Ji-Sook |
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Affiliation: | School of Chemical and Biological Engineering, Seoul National University, 599 Gwanangno, Gwanak-gu, Seoul 151-744, Republic of Korea |
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Abstract: | The accumulation of fibrillar form of α-synuclein (α-syn) has been implicated in Parkinson’s disease. Here we show that tubulin can stimulate α-syn fibrillization in vitro in different ways depending on its oligomeric status. The physiological significance of tubulin-seeded α-syn fibrillization is demonstrated by using Saccharomyces cerevisiae as a model system. Perturbation of microtubule system either by treating benomyl that inhibits microtubule assembly or by deleting genes involved in microtubule biogenesis, stimulates α-syn aggregation and toxicity. These results suggest that impairment of the microtubule system may act as a risk factor deteriorating the α-syn-mediated neurodegeneration by increasing the chance of tubulin-seeded α-syn aggregation. |
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Keywords: | α-Synuclein Amyloid Microtubule Tubulin Yeast model |
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