Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking - Wikidata - wikimedia - TriplyDB

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

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

http://www.wikidata.org/entity/Q37219276

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PINK1 is selectively stabilized on impaired mitochondria to activate Parkin Parkinson's disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402 Regulation of mitochondrial functions by protein phosphorylation and dephosphorylation Alterations in Mitochondrial Quality Control in Alzheimer's Disease MIRO GTPases in Mitochondrial Transport, Homeostasis and Pathology Novel subcellular localization for α-synuclein: possible functional consequences Cell signaling and mitochondrial dynamics: Implications for neuronal function and neurodegenerative disease The axonal transport of mitochondria Self and nonself: how autophagy targets mitochondria and bacteria Ageing and Parkinson's disease: why is advancing age the biggest risk factor?Emerging modes of PINK1 signaling: another task for MARK2 Genetics of Parkinson's disease - a clinical perspective Mitochondrial transport in neurons: impact on synaptic homeostasis and neurodegeneration.Structural coupling of the EF hand and C-terminal GTPase domains in the mitochondrial protein Miro Parkinson's disease as a result of aging PINK1 regulates histone H3 trimethylation and gene expression by interaction with the polycomb protein EED/WAIT1 Evidence for a common biological pathway linking three Parkinson's disease-causing genes: parkin, PINK1 and DJ-1 Mitochondrial trafficking in neurons Gene-environment interactions: key to unraveling the mystery of Parkinson's disease Beyond mitophagy: cytosolic PINK1 as a messenger of mitochondrial health PINK1-dependent recruitment of Parkin to mitochondria in mitophagy.PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65 Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin Microtubule affinity-regulating kinase 2 (MARK2) turns on phosphatase and tensin homolog (PTEN)-induced kinase 1 (PINK1) at Thr-313, a mutation site in Parkinson disease: effects on mitochondrial transport Axon degeneration and PGC-1α-mediated protection in a zebrafish model of α-synuclein toxicity Increasing microtubule acetylation rescues axonal transport and locomotor deficits caused by LRRK2 Roc-COR domain mutations.Lysine 27 ubiquitination of the mitochondrial transport protein Miro is dependent on serine 65 of the Parkin ubiquitin ligase Structural determinants of PINK1 topology and dual subcellular distribution A pivotal role for PINK1 and autophagy in mitochondrial quality control: implications for Parkinson disease.The mitochondrial Ras-related GTPase Miro: views from inside and outside the metazoan kingdom.Huntingtin protein is essential for mitochondrial metabolism, bioenergetics and structure in murine embryonic stem cells Retrograde axonal transport: pathways to cell death?Mitochondrial quality control mediated by PINK1 and Parkin: links to parkinsonism.The pallidopyramidal syndromes: nosology, aetiology and pathogenesis.Beyond the mitochondrion: cytosolic PINK1 remodels dendrites through protein kinase A Mitochondrial and Cell Death Mechanisms in Neurodegenerative Diseases.

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P2860

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

http://www.wikidata.org/entity/Q37219276

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on March 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Pink1 forms a multiprotein com ...... n to mitochondrial trafficking

@en

Pink1 forms a multiprotein com ...... to mitochondrial trafficking.

@nl

type

label

Pink1 forms a multiprotein com ...... n to mitochondrial trafficking

@en

Pink1 forms a multiprotein com ...... to mitochondrial trafficking.

@nl

altLabel

Pink1 Forms a Multiprotein Com ...... to Mitochondrial Trafficking†

@en

prefLabel

Pink1 forms a multiprotein com ...... n to mitochondrial trafficking

@en

Pink1 forms a multiprotein com ...... to mitochondrial trafficking.

@nl

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Pink1 forms a multiprotein com ...... n to mitochondrial trafficking

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Andreas Weihofen

http://www.w3.org/2001/XMLSchema#string

Beth L Ostaszewski

http://www.w3.org/2001/XMLSchema#string

Dennis J Selkoe

http://www.w3.org/2001/XMLSchema#string

Kelly Jean Thomas

http://www.w3.org/2001/XMLSchema#string

P2860

Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability

PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1

The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking

The kinase domain of mitochondrial PINK1 faces the cytoplasm

Atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis

Hereditary early-onset Parkinson's disease caused by mutations in PINK1

GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain proteins: association in vivo and in vitro with kinesin

The mitochondrial inner membrane protein mitofilin controls cristae morphology

Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway.

Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase

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2045-2052

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scholarly article

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10.1021/BI8019178

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9

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48

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2009-03-01T00:00:00Z

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19152501

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2693257

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