Poly-ADP-ribose assisted protein localization resolves that DJ-1, but not LRRK2 or α-synuclein, is localized to the mitochondrial matrix
| Autor: | Nelson Uchechukwu Osuagwu, Charalampos Tzoulis, Christian Dölle |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Poly Adenosine Diphosphate Ribose Physiology Protein Deglycase DJ-1 Mitochondrion Biochemistry Cell Fusion chemistry.chemical_compound 0302 clinical medicine Medicine and Health Sciences Energy-Producing Organelles Membrane Potential Mitochondrial Multidisciplinary Chemistry Parkinson Disease Transfection Protein subcellular localization prediction LRRK2 Recombinant Proteins Mitochondria Cell biology Subcellular Localization Electrophysiology Protein Transport Mitochondrial matrix Cytochemistry alpha-Synuclein Medicine Cellular Structures and Organelles Immunocytochemistry Research Article Cell Physiology Imaging Techniques Science Bioenergetics Research and Analysis Methods Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 Membrane Potential 03 medical and health sciences Fluorescence Imaging Ribose Humans Biology and Life Sciences Proteins Cell Biology Subcellular localization nervous system diseases 030104 developmental biology Mitochondrial Membrane 030217 neurology & neurosurgery |
| Zdroj: | PLoS ONE, Vol 14, Iss 7, p e0219909 (2019) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | 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. publishedVersion |
| Databáze: | OpenAIRE |
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