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000137272 0247_ $$2doi$$a10.1002/embj.201284290
000137272 0247_ $$2pmid$$apmid:24473149
000137272 0247_ $$2pmc$$apmc:PMC3983680
000137272 0247_ $$2ISSN$$a0261-4189
000137272 0247_ $$2ISSN$$a1460-2075
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000137272 037__ $$aDZNE-2020-03594
000137272 041__ $$aEnglish
000137272 082__ $$a570
000137272 1001_ $$aKlein, Pontus$$b0
000137272 245__ $$aRet rescues mitochondrial morphology and muscle degeneration of Drosophila Pink1 mutants.
000137272 260__ $$aHoboken, NJ [u.a.]$$bWiley$$c2014
000137272 264_1 $$2Crossref$$3online$$bWiley$$c2014-01-28
000137272 264_1 $$2Crossref$$3print$$bWiley$$c2014-02-18
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000137272 520__ $$aParkinson's disease (PD)-associated Pink1 and Parkin proteins are believed to function in a common pathway controlling mitochondrial clearance and trafficking. Glial cell line-derived neurotrophic factor (GDNF) and its signaling receptor Ret are neuroprotective in toxin-based animal models of PD. However, the mechanism by which GDNF/Ret protects cells from degenerating remains unclear. We investigated whether the Drosophila homolog of Ret can rescue Pink1 and park mutant phenotypes. We report that a signaling active version of Ret (Ret(MEN₂B) rescues muscle degeneration, disintegration of mitochondria and ATP content of Pink1 mutants. Interestingly, corresponding phenotypes of park mutants were not rescued, suggesting that the phenotypes of Pink1 and park mutants have partially different origins. In human neuroblastoma cells, GDNF treatment rescues morphological defects of PINK1 knockdown, without inducing mitophagy or Parkin recruitment. GDNF also rescues bioenergetic deficits of PINK knockdown cells. Furthermore, overexpression of Ret(MEN₂B) significantly improves electron transport chain complex I function in Pink1 mutant Drosophila. These results provide a novel mechanism underlying Ret-mediated cell protection in a situation relevant for human PD.
000137272 536__ $$0G:(DE-HGF)POF3-341$$a341 - Molecular Signaling (POF3-341)$$cPOF3-341$$fPOF III$$x0
000137272 542__ $$2Crossref$$i2015-09-01$$uhttp://doi.wiley.com/10.1002/tdm_license_1.1
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000137272 650_7 $$2NLM Chemicals$$aDrosophila Proteins
000137272 650_7 $$2NLM Chemicals$$aGlial Cell Line-Derived Neurotrophic Factor
000137272 650_7 $$08L70Q75FXE$$2NLM Chemicals$$aAdenosine Triphosphate
000137272 650_7 $$0EC 2.3.2.27$$2NLM Chemicals$$aUbiquitin-Protein Ligases
000137272 650_7 $$0EC 2.7.-$$2NLM Chemicals$$aProtein Kinases
000137272 650_7 $$0EC 2.7.10.1$$2NLM Chemicals$$aProto-Oncogene Proteins c-ret
000137272 650_7 $$0EC 2.7.10.1$$2NLM Chemicals$$aRet protein, Drosophila
000137272 650_7 $$0EC 2.7.11.1$$2NLM Chemicals$$aPINK1 protein, Drosophila
000137272 650_7 $$0EC 2.7.11.1$$2NLM Chemicals$$aPTEN-induced putative kinase
000137272 650_7 $$0EC 2.7.11.1$$2NLM Chemicals$$aProtein-Serine-Threonine Kinases
000137272 650_7 $$0EC 6.3.2.-$$2NLM Chemicals$$apark protein, Drosophila
000137272 650_7 $$0EC 7.1.1.2$$2NLM Chemicals$$aElectron Transport Complex I
000137272 650_7 $$0VTD58H1Z2X$$2NLM Chemicals$$aDopamine
000137272 650_2 $$2MeSH$$aAdenosine Triphosphate: metabolism
000137272 650_2 $$2MeSH$$aAnimals
000137272 650_2 $$2MeSH$$aApoptosis
000137272 650_2 $$2MeSH$$aAutophagy
000137272 650_2 $$2MeSH$$aCell Line, Tumor
000137272 650_2 $$2MeSH$$aDisease Models, Animal
000137272 650_2 $$2MeSH$$aDopamine: metabolism
000137272 650_2 $$2MeSH$$aDrosophila Proteins: deficiency
000137272 650_2 $$2MeSH$$aDrosophila Proteins: genetics
000137272 650_2 $$2MeSH$$aDrosophila Proteins: physiology
000137272 650_2 $$2MeSH$$aDrosophila melanogaster: genetics
000137272 650_2 $$2MeSH$$aDrosophila melanogaster: growth & development
000137272 650_2 $$2MeSH$$aElectron Transport Complex I: physiology
000137272 650_2 $$2MeSH$$aGenes, Lethal
000137272 650_2 $$2MeSH$$aGlial Cell Line-Derived Neurotrophic Factor: pharmacology
000137272 650_2 $$2MeSH$$aHumans
000137272 650_2 $$2MeSH$$aMitochondria, Muscle: ultrastructure
000137272 650_2 $$2MeSH$$aMuscular Atrophy: prevention & control
000137272 650_2 $$2MeSH$$aNeuroblastoma: pathology
000137272 650_2 $$2MeSH$$aNeurons: ultrastructure
000137272 650_2 $$2MeSH$$aOxygen Consumption
000137272 650_2 $$2MeSH$$aParkinson Disease
000137272 650_2 $$2MeSH$$aPhenotype
000137272 650_2 $$2MeSH$$aProtein Kinases: deficiency
000137272 650_2 $$2MeSH$$aProtein Kinases: genetics
000137272 650_2 $$2MeSH$$aProtein-Serine-Threonine Kinases: deficiency
000137272 650_2 $$2MeSH$$aProtein-Serine-Threonine Kinases: genetics
000137272 650_2 $$2MeSH$$aProtein-Serine-Threonine Kinases: physiology
000137272 650_2 $$2MeSH$$aProto-Oncogene Proteins c-ret: genetics
000137272 650_2 $$2MeSH$$aProto-Oncogene Proteins c-ret: physiology
000137272 650_2 $$2MeSH$$aPupa
000137272 650_2 $$2MeSH$$aSignal Transduction: physiology
000137272 650_2 $$2MeSH$$aUbiquitin-Protein Ligases: deficiency
000137272 650_2 $$2MeSH$$aUbiquitin-Protein Ligases: genetics
000137272 7001_ $$0P:(DE-2719)9000425$$aMüller-Rischart, Anne Kathrin$$b1$$udzne
000137272 7001_ $$aMotori, Elisa$$b2
000137272 7001_ $$aSchönbauer, Cornelia$$b3
000137272 7001_ $$aSchnorrer, Frank$$b4
000137272 7001_ $$0P:(DE-2719)9000369$$aWinklhofer, Konstanze F$$b5$$udzne
000137272 7001_ $$0P:(DE-HGF)0$$aKlein, Rüdiger$$b6$$eCorresponding author
000137272 77318 $$2Crossref$$3journal-article$$a10.1002/embj.201284290$$b : Wiley, 2014-01-28$$n4$$p341-355$$tThe EMBO Journal$$v33$$x0261-4189$$y2014
000137272 773__ $$0PERI:(DE-600)1467419-1$$a10.1002/embj.201284290$$gVol. 33, no. 4, p. 341 - 355$$n4$$p341-355$$q33:4<341 - 355$$tThe EMBO journal$$v33$$x0261-4189$$y2014
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000137272 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3983680
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