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The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Open accessAbstract
Understanding the function of genes mutated in hereditary forms of Parkinson's disease yields insight into disease etiology and reveals new pathways in cell biology. Although mutations or variants in many genes increase the susceptibility to Parkinson's disease, only a handful of monogenic causes of parkinsonism have been identified. Biochemical and genetic studies reveal that the products of two genes that are mutated in autosomal recessive parkinsonism, PINK1 and Parkin, normally work together in the same pathway to govern mitochondrial quality control, bolstering previous evidence that mitochondrial damage is involved in Parkinson's disease. PINK1 accumulates on the outer membrane of damaged mitochondria, activates Parkin's E3 ubiquitin ligase activity, and recruits Parkin to the dysfunctional mitochondrion. Then, Parkin ubiquitinates outer mitochondrial membrane proteins to trigger selective autophagy. This review covers the normal functions that PINK1 and Parkin play within cells, their molecular mechanisms of action, and the pathophysiological consequences of their loss.
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“PINK1 plays critical roles in mitochondrial quality control, particularly in induction of mitophagy [39].”
From miR-27a and miR-27b regulate autophagic clearance of damaged mitochondria by targeting PTEN-induced putative kinase 1 (PINK1) (2016) · cites this paper as [39]
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“In PD or AD, only a minor subset of patients has a genetic mutation responsible for disease development (e.g., SNCA , PINK1 and PARK2 mutations in PD (Abeliovich and Gitler, 2016)(Pickrell and Youle, 2015), and APP, PSEN1, PSEN2 in AD (Van Cauwenberghe et al., 2016)).”
From TET2 Regulates the Neuroinflammatory Response in Microglia (2019) · cites this paper as Pickrell and Youle, 2015
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The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
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Image-based genome-wide siRNA screen identifies selective autophagy factors
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Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner
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Susceptibility to leprosy is associated with PARK2 and PACRG
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The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway
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p62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding
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PTEN-inducible kinase 1 (PINK1)/Park6 is indispensable for normal heart function
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Self-citationAMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1
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p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria
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“Although an initial report indicated that p62 is required for Parkin-mediated mitophagy (Geisler et al., 2010a), two groups using p62-KOmouse embryonic fibroblasts did not find that it is essential for mitophagy (Narendra et al., 2010a; Okatsu et al., 2010).”
BackgroundThe mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking
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Parkin and PINK1: much more than mitophagy
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Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway
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Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases
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USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin
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Vitamin K 2 Is a Mitochondrial Electron Carrier That Rescues Pink1 Deficiency
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High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy
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Self-citationMitochondrial Quality Control Mediated by PINK1 and Parkin: Links to ParkinsonismPreprint
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Self-citationLoss of locus coeruleus neurons and reduced startle in parkin null mice
von Coelln, R., Thomas, B., Savitt, J. M., Lim, K. L., Sasaki, M., Hess, E. J., Dawson, V. L., & Dawson, T. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401297101 · Cited by 353
Sulfhydration mediates neuroprotective actions of parkin
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Preconditioning Involves Selective Mitophagy Mediated by Parkin and p62/SQSTM1
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Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells
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Self-citationAutoregulation of Parkin activity through its ubiquitin‐like domain
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The genetics and neuropathology of Parkinson’s disease
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Structure of the human Parkin ligase domain in an autoinhibited state
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The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy
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The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations
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“Although an initial report indicated that p62 is required for Parkin-mediated mitophagy (Geisler et al., 2010a), two groups using p62-KOmouse embryonic fibroblasts did not find that it is essential for mitophagy (Narendra et al., 2010a; Okatsu et al., 2010).”
BackgroundInfluentialMitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy
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Parkin Interacts with Ambra1 to Induce Mitophagy
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“Affinity-binding studies indicate that AMBRA1, a protein involved in autophagy, binds to Parkin and promotes mitophagy (Van Humbeeck et al., 2011).”
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A neo-substrate that amplifies catalytic activity of Parkinson's-disease-related kinase PINK1
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Absence of nigral degeneration in aged parkin/DJ‐1/PINK1 triple knockout mice
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Mutant A53T α-Synuclein Induces Neuronal Death by Increasing Mitochondrial Autophagy
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Characterization of PINK1 processing, stability, and subcellular localization
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Parkin negatively regulates JNK pathway in the dopaminergic neurons of Drosophila
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The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy
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A Dimeric PINK1-containing Complex on Depolarized Mitochondria Stimulates Parkin Recruitment
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PINK1-linked parkinsonism is associated with Lewy body pathology
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Mitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage
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Lewy body Parkinson's disease in a large pedigree with 77Parkin mutation carriers
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Mutations in PINK1 and Parkin Impair Ubiquitination of Mitofusins in Human Fibroblasts
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PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding
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Phenotypic characterization of recessive gene knockout rat models of Parkinson's disease
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Piecemeal Microautophagy of the Nucleus Requires the Core Macroautophagy Genes
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Mutations in Fis1 disrupt orderly disposal of defective mitochondria
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Self-citationParkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation
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The E3 Ligase Parkin Maintains Mitochondrial Integrity by Increasing Linear Ubiquitination of NEMO
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Depletion of PINK1 affects mitochondrial metabolism, calcium homeostasis and energy maintenance
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The ubiquitin E3 ligase parkin regulates the proapoptotic function of Bax
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Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission
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The PINK1–Parkin pathway is involved in the regulation of mitochondrial remodeling process
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Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage
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Point Mutations (Thr240Arg and Ala311Stop) in theParkinGene
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Self-citationThe Yeast Complex I Equivalent NADH Dehydrogenase Rescues pink1 Mutants
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Park6‐linked parkinsonism occurs in several european families
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Self-citationPINK1 Triggers Autocatalytic Activation of Parkin to Specify Cell Fate Decisions
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Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
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Hexokinase activity is required for recruitment of parkin to depolarized mitochondria
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The Impact of Pathogenic Mitochondrial DNA Mutations on Substantia Nigra Neurons
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3 of the 212 references couldn’t be matched to a known paper.
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Self-citation
Metadata
- Authors
- Pickrell, A. M., & Youle, R. J.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Youle, Richard J.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2015-01
- Volume
- 85
- Issue
- 2
- Pages
- 257-273
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC4764997
- OpenAlex
- W2082425146
- Cited by
- 2,310
- References
- 212
- Citations by year
- 2026: 268 · 2025: 234 · 2024: 177 · 2023: 175 · 2022: 228 · 2021: 261 · 2020: 239 · 2019: 197 · 2018: 178 · 2017: 174 · 2016: 123 · 2015: 54
- FWCI
- 23.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences
- National Institute of Neurological Disorders and Stroke (Z01NS002859)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- PINK1, Parkin, Parkinson's disease, mitochondrial quality control, mitochondrial damage, E3 ubiquitin ligase, selective autophagy, mitophagy, autosomal recessive parkinsonism, mitochondrial outer membrane
- MeSH terms
- PTEN-Induced Putative Kinase, Humans, Mitochondria, Parkinson Disease, Protein Kinases, Parkinsonian Disorders, Ubiquitin-Protein Ligases, Proteolysis, Mitophagy
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