Journal article

Oligomeric alpha-synuclein inhibits tubulin polymerization

Leo Chen, Jinghua Jin, Jeanne Davis, Yong Zhou, Yan Wang, Jun Liu, Paul J Lockhart, Jing Zhang

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2007

Abstract

Earlier investigations have demonstrated that tubulin co-localizes with alpha-synuclein in Lewy bodies and influences the formation of alpha-synuclein aggregation. However, it is not clear whether aggregated alpha-synuclein has any effects on the function of tubulin, i.e. tubulin polymerization, a critical mechanism by which neurons maintain their morphology and execute functions. In this study, we evaluated the effects of aggregated alpha-synuclein on tubulin polymerization in dopaminergic neurons (MES cells), along with mitochondrial function, cell morphology, and viability. The results indicate that MES cells exposed to extracellular oligomeric alpha-synuclein exhibited decreased tubulin ..

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