Title |
Molecular interaction of α-synuclein with tubulin influences on the polymerization of microtubule in vitro and structure of microtubule in cells
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Published in |
Molecular Biology Reports, October 2009
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DOI | 10.1007/s11033-009-9899-2 |
Pubmed ID | |
Authors |
R. M. Zhou, Y. X. Huang, X. L. Li, C. Chen, Q. Shi, G. R. Wang, C. Tian, Z. Y. Wang, Y. Y. Jing, C. Gao, X. P. Dong |
Abstract |
Microtubule dynamics is essential for many vital cellular processes such as in intracellular transport, metabolism, and cell division. Evidences demonstrate that α-synuclein may associate with microtubular cytoskeleton and its major component, tubulin. In the present study, the molecular interaction between α-synuclein and tubulin was confirmed by GST pull-down assay and co-immunoprecipitation. The interacting regions within α-synuclein with tubulin were mapped at the residues 60-100 of α-synuclein that is critical for the binding activity with tubulin. Microtubule assembly assays and sedimentation tests demonstrated that α-synuclein influenced the polymerization of tubulin in vitro, revealing an interacting region-dependent feature. Confocal microscopy detected that exposures of α-synuclein proteins inhibited microtubule formation in the cultured cells, with a length-dependent phenomenon. Our data highlight a potential role of α-synuclein in regulating the microtubule dynamics in neurons. The association of α-synuclein with tubulin may further provide insight into the biological and pathophysiological function of synuclein. |
Mendeley readers
Geographical breakdown
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Demographic breakdown
Readers by professional status | Count | As % |
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Student > Master | 12 | 12% |
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Researcher | 12 | 12% |
Other | 3 | 3% |
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Unknown | 28 | 29% |
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Pharmacology, Toxicology and Pharmaceutical Science | 4 | 4% |
Other | 6 | 6% |
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