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Distinct Mechanisms of Pathogenic DJ-1 Mutations in Mitochondrial Quality Control
Journal article   Open access   Peer reviewed

Distinct Mechanisms of Pathogenic DJ-1 Mutations in Mitochondrial Quality Control

Daniela Strobbe, Alexis A Robinson, Kirsten Harvey, Lara Rossi, Caterina Ferranina, Valerio de Biase, Carlo Rodolfo, Robert J Harvey and Michelangelo Campanella
Frontiers in Molecular Neuroscience, Vol.11, 68
2018
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https://doi.org/10.3389/fnmol.2018.00068View
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Abstract

mitochondria mitophagy DJ-1 DJBP/EFCAB6 PARK7 SUMO-1
The deglycase and chaperone protein DJ-1 is pivotal for cellular oxidative stress responses and mitochondrial quality control. Mutations in PARK7, encoding DJ-1, are associated with early-onset familial Parkinson's disease and lead to pathological oxidative stress and/or disrupted protein degradation by the proteasome. The aim of this study was to gain insights into the pathogenic mechanisms of selected DJ-1 missense mutations, by characterizing protein-protein interactions, core parameters of mitochondrial function, quality control regulation via autophagy, and cellular death following dopamine accumulation. We report that the DJ-1M26I mutant influences DJ-1 interactions with SUMO-1, in turn enhancing removal of mitochondria and conferring increased cellular susceptibility to dopamine toxicity. By contrast, the DJ-1D149A mutant does not influence mitophagy, but instead impairs Ca2+ dynamics and free radical homeostasis by disrupting DJ-1 interactions with a mitochondrial accessory protein known as DJ-1-binding protein (DJBP/EFCAB6). Thus, individual DJ-1 mutations have different effects on mitochondrial function and quality control, implying mutation-specific pathomechanisms converging on impaired mitochondrial homeostasis.

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