. Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration. Proc Natl Acad Sci U S A. 2012 Jun 12;109(24):9611-6. PubMed.

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  1. Gitler et al. (see ARF related news story) previously demonstrated that ATP13A2/PARK9 functionally modified α-synuclein toxicity in yeast, and that its overexpression protected dopamine neurons in C. elegans from age-dependent α-synuclein degeneration. This excellent new study from Dehay and colleagues provides strong support for the hypothesis that ATP13A2/PARK9 activity is important for efficient lysosomal function and protein degradation. In the context of the growing literature on the shared cellular dysfunction underlying Gaucher's disease and Parkinson's disease (Mazzulli et al., 2011), these results extend the prospect that therapeutic interventions directed at enhancement of lysosomal-autophagy pathways represent an important target for PD research. The identification of genetic and protein modifiers of ATP13A2 activity may serve to elucidate additional mechanistic insights that can expand the potential for such therapies.

    References:

    . Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell. 2011 Jul 8;146(1):37-52. PubMed.

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  1. Evidence Piles Up for Lysosomal Dysfunction in Parkinson’s