Functional interplay between Parkin and Drp1 in mitochondrial fission and clearance.
Identifieur interne : 001414 ( Ncbi/Checkpoint ); précédent : 001413; suivant : 001415Functional interplay between Parkin and Drp1 in mitochondrial fission and clearance.
Auteurs : Lori Buhlman [États-Unis] ; Maria Damiano [France] ; Giulia Bertolin [France] ; Rosa Ferrando-Miguel [France] ; Anne Lombès [France] ; Alexis Brice [France] ; Olga Corti [France]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2014.
English descriptors
- KwdEn :
- Animals, COS Cells, Cercopithecus aethiops, Dynamins (metabolism), Humans, Mitochondria (metabolism), Mitochondrial Degradation, Mitochondrial Dynamics, Mitochondrial Proteins (metabolism), Mutation (genetics), Parkinson Disease (genetics), Phosphorylation, Protein Binding, Protein Kinases (metabolism), Protein Structure, Quaternary, Signal Transduction, Ubiquitin-Protein Ligases (metabolism).
- MESH :
- chemical , metabolism : Dynamins, Mitochondrial Proteins, Protein Kinases, Ubiquitin-Protein Ligases.
- genetics : Mutation, Parkinson Disease.
- metabolism : Mitochondria.
- Animals, COS Cells, Cercopithecus aethiops, Humans, Mitochondrial Degradation, Mitochondrial Dynamics, Phosphorylation, Protein Binding, Protein Structure, Quaternary, Signal Transduction.
Abstract
Autosomal recessive early-onset Parkinson's disease is most often caused by mutations in the genes encoding the cytosolic E3 ubiquitin ligase Parkin and the mitochondrial serine/threonine kinase PINK1. Studies in Drosophila models and mammalian cells have demonstrated that these proteins regulate various aspects of mitochondrial physiology, including organelle transport, dynamics and turnover. How PINK1 and Parkin orchestrate these processes, and whether they always do so within a common pathway remain to be clarified. We have revisited the role of PINK1 and Parkin in mitochondrial dynamics, and explored its relation to the mitochondrial clearance program controlled by these proteins. We show that PINK1 and Parkin promote Drp1-dependent mitochondrial fission by mechanisms that are at least in part independent. Parkin-mediated mitochondrial fragmentation was abolished by treatments interfering with the calcium/calmodulin/calcineurin signaling pathway, suggesting that it requires dephosphorylation of serine 637 of Drp1. Parkinson's disease-causing mutations with differential impact on mitochondrial morphology and organelle degradation demonstrated that the pro-fission effect of Parkin is not required for efficient mitochondrial clearance. In contrast, the use of Förster energy transfer imaging microscopy revealed that Drp1 and Parkin are co-recruited to mitochondria in proximity of PINK1 following mitochondrial depolarization, indicating spatial coordination between these events in mitochondrial degradation. Our results also hint at a major role of the outer mitochondrial adaptor MiD51 in Drp1 recruitment and Parkin-dependent mitophagy. Altogether, our observations provide new insight into the mechanisms underlying the regulation of mitochondrial dynamics by Parkin and its relation to the mitochondrial clearance program mediated by the PINK1/Parkin pathway.
DOI: 10.1016/j.bbamcr.2014.05.012
PubMed: 24878071
Affiliations:
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<front><div type="abstract" xml:lang="en">Autosomal recessive early-onset Parkinson's disease is most often caused by mutations in the genes encoding the cytosolic E3 ubiquitin ligase Parkin and the mitochondrial serine/threonine kinase PINK1. Studies in Drosophila models and mammalian cells have demonstrated that these proteins regulate various aspects of mitochondrial physiology, including organelle transport, dynamics and turnover. How PINK1 and Parkin orchestrate these processes, and whether they always do so within a common pathway remain to be clarified. We have revisited the role of PINK1 and Parkin in mitochondrial dynamics, and explored its relation to the mitochondrial clearance program controlled by these proteins. We show that PINK1 and Parkin promote Drp1-dependent mitochondrial fission by mechanisms that are at least in part independent. Parkin-mediated mitochondrial fragmentation was abolished by treatments interfering with the calcium/calmodulin/calcineurin signaling pathway, suggesting that it requires dephosphorylation of serine 637 of Drp1. Parkinson's disease-causing mutations with differential impact on mitochondrial morphology and organelle degradation demonstrated that the pro-fission effect of Parkin is not required for efficient mitochondrial clearance. In contrast, the use of Förster energy transfer imaging microscopy revealed that Drp1 and Parkin are co-recruited to mitochondria in proximity of PINK1 following mitochondrial depolarization, indicating spatial coordination between these events in mitochondrial degradation. Our results also hint at a major role of the outer mitochondrial adaptor MiD51 in Drp1 recruitment and Parkin-dependent mitophagy. Altogether, our observations provide new insight into the mechanisms underlying the regulation of mitochondrial dynamics by Parkin and its relation to the mitochondrial clearance program mediated by the PINK1/Parkin pathway.</div>
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