Regulation of ATP13A2 via PHD2-HIF1α Signaling Is Critical for Cellular Iron Homeostasis: Implications for Parkinson's Disease (Q28118364)

2 July 2019

title

Regulation of ATP13A2 via PHD2-HIF1α Signaling Is Critical for Cellular Iron Homeostasis: Implications for Parkinson's Disease (English)

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2 July 2019

ATPase cation transporting 13A2

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cellular iron ion homeostasis

GOA release 2020-03-11

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Egl-9 family hypoxia-inducible factor 1

GOA release 2020-03-11

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GOA release 2020-03-11

author

Julie K Andersen

4

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2 July 2019

author name string

Subramanian Rajagopalan

1

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2 July 2019

Anand Rane

2

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2 July 2019

Shankar J Chinta

3

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2 July 2019

language of work or name

English

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publication date

1 January 2016

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2 July 2019

published in

Journal of Neuroscience

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2 July 2019

volume

36

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2 July 2019

issue

4

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2 July 2019

page(s)

1086-1095

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2 July 2019

A conserved family of prolyl-4-hydroxylases that modify HIF

cites work

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Genetic or pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: a novel therapy for Parkinson's disease

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Intralysosomal iron chelation protects against oxidative stress-induced cellular damage.

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Lack of hypoxia-inducible factor-1 alpha impairs midbrain neural precursor cells involving vascular endothelial growth factor signaling

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Does the calcein-AM method assay the total cellular 'labile iron pool' or only a fraction of it?

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Regulation of adult erythropoiesis by prolyl hydroxylase domain proteins

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Inducible alterations of glutathione levels in adult dopaminergic midbrain neurons result in nigrostriatal degeneration.

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Lysosomes in iron metabolism, ageing and apoptosis

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Translocation of iron from lysosomes into mitochondria is a key event during oxidative stress-induced hepatocellular injury

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Divalent metal transporter 1 (DMT1) contributes to neurodegeneration in animal models of Parkinson's disease

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Inhibition of prolyl hydroxylase protects against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity: model for the potential involvement of the hypoxia-inducible factor pathway in Parkinson disease

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Chronic expression of H-ferritin in dopaminergic midbrain neurons results in an age-related expansion of the labile iron pool and subsequent neurodegeneration: implications for Parkinson's disease.

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Prolyl hydroxylase domain inhibitors: a route to HIF activation and neuroprotection

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Cellular signal transduction of the hypoxia response

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Lysosomal iron mobilization and induction of the mitochondrial permeability transition in acetaminophen-induced toxicity to mouse hepatocytes.

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Hypoxia. 1. Intracellular sensors for oxygen and oxidative stress: novel therapeutic targets

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Expression analysis of dopaminergic neurons in Parkinson's disease and aging links transcriptional dysregulation of energy metabolism to cell death.

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Pathogenic effects of novel mutations in the P-type ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset parkinsonism

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The role of lysosomes in iron metabolism and recycling

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ATP13A2 regulates mitochondrial bioenergetics through macroautophagy

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Hypoxia regulation of ATP13A2 (PARK9) gene transcription

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ATP13A2 mutations impair mitochondrial function in fibroblasts from patients with Kufor-Rakeb syndrome.

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Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration.

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Analysis of synaptic vesicle endocytosis in synaptosomes by high-content screening.

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Common pathogenic effects of missense mutations in the P-type ATPase ATP13A2 (PARK9) associated with early-onset parkinsonism

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Lysosomal iron, iron chelation, and cell death

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Pharmacological prolyl hydroxylase domain inhibition as a therapeutic target for Parkinson's disease

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ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

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Zn²⁺ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation

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Parkinson's disease-associated human ATP13A2 (PARK9) deficiency causes zinc dyshomeostasis and mitochondrial dysfunction

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Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes

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Neurodegeneration with brain iron accumulation: update on pathogenic mechanisms

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ATP13A2/PARK9 regulates secretion of exosomes and α-synuclein

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α-Synuclein-independent histopathological and motor deficits in mice lacking the endolysosomal Parkinsonism protein Atp13a2.

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The Parkinson-associated human P5B-ATPase ATP13A2 protects against the iron-induced cytotoxicity.

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Differential degradation of motor deficits during gradual dopamine depletion with 6-hydroxydopamine in mice.

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10.1523/JNEUROSCI.3117-15.2016

Identifiers

DOI

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2 July 2019

PMCID

6404282

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2 July 2019

PubMed ID

26818499

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2 July 2019