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. 2008 Jul 2;28(27):6757-9.
doi: 10.1523/JNEUROSCI.1870-08.2008.

Heat shock protein 90 modulates LRRK2 stability: potential implications for Parkinson's disease treatment

Andrés Hurtado-Lorenzo  1 , Vasanti S Anand
Affiliations

Heat shock protein 90 modulates LRRK2 stability: potential implications for Parkinson's disease treatment

Andrés Hurtado-Lorenzo et al. J Neurosci. .
No abstract available

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Figures

Figure 1.
Figure 1.
Model of Hsp90-mediated LRRK2 stability. Hsp90–cdc37 complex binds to and stabilizes LRRK2 protein. Inhibition of Hsp90 chaperone activity with geldanamycin (GA) or PU-H71 disrupts these interactions and promotes the binding of LRRK2 to Hsc70, leading to proteasomal degradation of LRRK2.
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