Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy.
Identifieur interne : 000660 ( PubMed/Corpus ); précédent : 000659; suivant : 000661Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy.
Auteurs : Karl Grenier ; Maria Kontogiannea ; Edward A. FonSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2014.
English descriptors
- KwdEn :
- Animals, Cyclin-Dependent Kinase Inhibitor p16 (metabolism), Enzyme Stability, HEK293 Cells, HeLa Cells, Humans, Membrane Potential, Mitochondrial, Mice, Mitochondria (metabolism), Mitochondrial Degradation, Neurons (metabolism), Protein Kinases (metabolism), Protein Transport, Rats, Ubiquitin-Protein Ligases (metabolism).
- MESH :
- chemical , metabolism : Cyclin-Dependent Kinase Inhibitor p16, Protein Kinases, Ubiquitin-Protein Ligases.
- metabolism : Mitochondria, Neurons.
- Animals, Enzyme Stability, HEK293 Cells, HeLa Cells, Humans, Membrane Potential, Mitochondrial, Mice, Mitochondrial Degradation, Protein Transport, Rats.
Abstract
Parkinson disease (PD) is a complex neurodegenerative disease characterized by the loss of dopaminergic neurons in the substantia nigra. Multiple genes have been associated with PD, including Parkin and PINK1. Recent studies have established that the Parkin and PINK1 proteins function in a common mitochondrial quality control pathway, whereby disruption of the mitochondrial membrane potential leads to PINK1 stabilization at the mitochondrial outer surface. PINK1 accumulation leads to Parkin recruitment from the cytosol, which in turn promotes the degradation of the damaged mitochondria by autophagy (mitophagy). Most studies characterizing PINK1/Parkin mitophagy have relied on high concentrations of chemical uncouplers to trigger mitochondrial depolarization, a stimulus that has been difficult to adapt to neuronal systems and one unlikely to faithfully model the mitochondrial damage that occurs in PD. Here, we report that the short mitochondrial isoform of ARF (smARF), previously identified as an alternate translation product of the tumor suppressor p19ARF, depolarizes mitochondria and promotes mitophagy in a Parkin/PINK1-dependent manner, both in cell lines and in neurons. The work positions smARF upstream of PINK1 and Parkin and demonstrates that mitophagy can be triggered by intrinsic signaling cascades.
DOI: 10.1074/jbc.M114.607150
PubMed: 25217637
Links to Exploration step
pubmed:25217637Le document en format XML
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<affiliation><nlm:affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.</nlm:affiliation>
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<author><name sortKey="Kontogiannea, Maria" sort="Kontogiannea, Maria" uniqKey="Kontogiannea M" first="Maria" last="Kontogiannea">Maria Kontogiannea</name>
<affiliation><nlm:affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.</nlm:affiliation>
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<author><name sortKey="Fon, Edward A" sort="Fon, Edward A" uniqKey="Fon E" first="Edward A" last="Fon">Edward A. Fon</name>
<affiliation><nlm:affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada ted.fon@mcgill.ca.</nlm:affiliation>
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<term>HeLa Cells</term>
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<front><div type="abstract" xml:lang="en">Parkinson disease (PD) is a complex neurodegenerative disease characterized by the loss of dopaminergic neurons in the substantia nigra. Multiple genes have been associated with PD, including Parkin and PINK1. Recent studies have established that the Parkin and PINK1 proteins function in a common mitochondrial quality control pathway, whereby disruption of the mitochondrial membrane potential leads to PINK1 stabilization at the mitochondrial outer surface. PINK1 accumulation leads to Parkin recruitment from the cytosol, which in turn promotes the degradation of the damaged mitochondria by autophagy (mitophagy). Most studies characterizing PINK1/Parkin mitophagy have relied on high concentrations of chemical uncouplers to trigger mitochondrial depolarization, a stimulus that has been difficult to adapt to neuronal systems and one unlikely to faithfully model the mitochondrial damage that occurs in PD. Here, we report that the short mitochondrial isoform of ARF (smARF), previously identified as an alternate translation product of the tumor suppressor p19ARF, depolarizes mitochondria and promotes mitophagy in a Parkin/PINK1-dependent manner, both in cell lines and in neurons. The work positions smARF upstream of PINK1 and Parkin and demonstrates that mitophagy can be triggered by intrinsic signaling cascades.</div>
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<Abstract><AbstractText>Parkinson disease (PD) is a complex neurodegenerative disease characterized by the loss of dopaminergic neurons in the substantia nigra. Multiple genes have been associated with PD, including Parkin and PINK1. Recent studies have established that the Parkin and PINK1 proteins function in a common mitochondrial quality control pathway, whereby disruption of the mitochondrial membrane potential leads to PINK1 stabilization at the mitochondrial outer surface. PINK1 accumulation leads to Parkin recruitment from the cytosol, which in turn promotes the degradation of the damaged mitochondria by autophagy (mitophagy). Most studies characterizing PINK1/Parkin mitophagy have relied on high concentrations of chemical uncouplers to trigger mitochondrial depolarization, a stimulus that has been difficult to adapt to neuronal systems and one unlikely to faithfully model the mitochondrial damage that occurs in PD. Here, we report that the short mitochondrial isoform of ARF (smARF), previously identified as an alternate translation product of the tumor suppressor p19ARF, depolarizes mitochondria and promotes mitophagy in a Parkin/PINK1-dependent manner, both in cell lines and in neurons. The work positions smARF upstream of PINK1 and Parkin and demonstrates that mitophagy can be triggered by intrinsic signaling cascades.</AbstractText>
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