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Previous Article | Next Article
The Journal of Neuroscience, April 15, 2003, 23(8):3316
Parkin Binds to
/
Tubulin and Increases their Ubiquitination and Degradation
Yong Ren, Jinghui Zhao, and Jian Feng Department of Physiology and Biophysics, State University of New York at Buffalo, Buffalo, New York 14214
In addition to inhibiting the mitochondrial respiratory chain, toxins known to cause Parkinson's disease (PD), such as 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and rotenone, also strongly depolymerize microtubules and increase tubulin degradation. Microtubules are polymers of tubulin
/
heterodimers, whose correct folding requires coordinated actions of cellular chaperonins and cofactors. Misfolded tubulin monomers are highly toxic and quickly degraded through a hitherto unknown mechanism. Here we report that parkin, a protein-ubiquitin E3 ligase linked to PD, was tightly bound to microtubules in taxol-mediated microtubule coassembly assays. In lysates from the rat brain or transfected human embryonic kidney (HEK) 293 cells,
Key words: parkin; Parkinson's disease; tubulin; ubiquitination; misfolding; microtubule; dopamine
Copyright © 2003 Society for Neuroscience 0270-6474/03/2383316-09$05.00/0
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