Mitophagy and Parkinson's disease: be eaten to stay healthy.

No abstract is available for this paper.

• Publication year

  2013

• Venue

  Molecular and cellular neurosciences

• Publication date

  2013-07-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/j.mcn.2012.07.008PMID 22926193
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy

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• Pink1 Kinase and Its Membrane Potential (Δψ)-dependent Cleavage Product Both Localize to Outer Mitochondrial Membrane by Unique Targeting Mode*

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• Parkin, PINK1 and mitochondrial integrity: emerging concepts of mitochondrial dysfunction in Parkinson’s disease

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• Parkinson's Disease–Associated Kinase PINK1 Regulates Miro Protein Level and Axonal Transport of Mitochondria

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• Mitochondrial Contribution to Parkinson's Disease Pathogenesis

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• Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization.

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• Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1

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• The role of calcium and mitochondrial oxidant stress in the loss of substantia nigra pars compacta dopaminergic neurons in Parkinson's disease.

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• Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo

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• PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility.

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• Silencing of PINK1 induces mitophagy via mitochondrial permeability transition in dopaminergic MN9D cells.

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• The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons.

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• Mitochondrially localized PKA reverses mitochondrial pathology and dysfunction in a cellular model of Parkinson's disease

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• Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling.

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• Genetic Etiology of Parkinson Disease Associated with Mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 Genes: A Mutation Update

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• The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy

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• Perturbations in Mitochondrial Dynamics Induced by Human Mutant PINK1 Can Be Rescued by the Mitochondrial Division Inhibitor mdivi-1*

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• p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both

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• p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria

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• PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy

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• Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL

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• Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy.

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• Disease-causing mutations in Parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy

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• The molecular machinery of autophagy and its role in physiology and disease.

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• PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

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• Nix Is Critical to Two Distinct Phases of Mitophagy, Reactive Oxygen Species-mediated Autophagy Induction and Parkin-Ubiquitin-p62-mediated Mitochondrial Priming*

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• The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway

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• PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

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• Reduction of Protein Translation and Activation of Autophagy Protect against PINK1 Pathogenesis in Drosophila melanogaster

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• Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin

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• Molecular pathogenesis of Parkinson disease: insights from genetic studies

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• Role of BNIP3 and NIX in cell death, autophagy, and mitophagy

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• Loss of Parkin or PINK1 Function Increases Drp1-dependent Mitochondrial Fragmentation*

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• Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking.

  2009cited by this paper
• Parkin stabilizes PINK1 through direct interaction.

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• Loss of PINK1 Function Promotes Mitophagy through Effects on Oxidative Stress and Mitochondrial Fission*

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• PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

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• The kinase domain of mitochondrial PINK1 faces the cytoplasm

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• Characterization of PINK1 processing, stability, and subcellular localization

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• PINK1 controls mitochondrial localization of Parkin through direct phosphorylation.

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• The PINK1/Parkin pathway regulates mitochondrial morphology

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• Fission and selective fusion govern mitochondrial segregation and elimination by autophagy

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• Expression of PINK1 mRNA in human and rodent brain and in Parkinson's disease.

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• NIX is required for programmed mitochondrial clearance during reticulocyte maturation

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• p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy*

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• Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.

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• Loss-of-Function of Human PINK1 Results in Mitochondrial Pathology and Can Be Rescued by Parkin

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• Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin

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• Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin

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• Epidemiology of Parkinson's disease.

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• High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease

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• Glycolysis: The Next Big Breakthrough in Parkinson’s Disease

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• Putting the Brakes on Autophagy: The role of Heparan Sulfate Modified Proteins in the Balance of Anabolic and Catabolic Pathways and Intracellular Quality Control.

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• Exogenous Alpha-Synuclein Evoked Parkin Downregulation Promotes Mitochondrial Dysfunction in Neuronal Cells. Implications for Parkinson’s Disease Pathology

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• Research Progress on the Mechanism of Mitochondrial Autophagy in Cerebral Stroke

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