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PLoS One. 2019 Jul 19;14(7):e0219909. doi: 10.1371/journal.pone.0219909. eCollection 2019.

Poly-ADP-ribose assisted protein localization resolves that DJ-1, but not LRRK2 or α-synuclein, is localized to the mitochondrial matrix.

Osuagwu N1,2,3, Dölle C1,2,3, Tzoulis C1,2,3.

Author information

1
Department of Clinical Medicine, University of Bergen, Bergen, Norway.
2
Department of Neurology, Haukeland University Hospital, Bergen, Norway.
3
Neuro-SysMed Center of Excellence for Clinical Research in Neurological Diseases, Haukeland University Hospital and University of Bergen, Bergen, Norway.

Abstract

Several proteins linked to familial Parkinson disease have been associated with mitochondrial (dys-)function and have been described to reside within mitochondria. The putative mitochondrial and sub-mitochondrial localization of these proteins remains disputed, however, potentially due to conflicting results obtained by diverging technical approaches. Using the high-resolution poly-ADP-ribose assisted protein localization assay that also allows for detection of low level and even partial mitochondrial matrix localization, we demonstrate here that DJ-1, but not LRRK2 or α-synuclein, resides in the mitochondrial matrix. The localization of the proteins was not changed in cellular stress models of Parkinson disease and, in case of α-synuclein, not affected by pathological mutations. Our results verify the ability of DJ-1 to carry out its role also from within mitochondria and suggest that LRRK2 and α-synuclein may interact with and affect mitochondria from outside the mitochondrial matrix.

Conflict of interest statement

The authors have declared that no competing interests exist.

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