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000136119 0247_ $$2doi$$a10.4161/auto.6.7.13286
000136119 0247_ $$2pmid$$apmid:20798600
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000136119 037__ $$aDZNE-2020-02441
000136119 041__ $$aEnglish
000136119 082__ $$a570
000136119 1001_ $$0P:(DE-HGF)0$$aGeisler, Sven$$b0
000136119 245__ $$aThe PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations.
000136119 260__ $$aAbingdon, Oxon$$bTaylor & Francis$$c2010
000136119 264_1 $$2Crossref$$3online$$bInforma UK Limited$$c2014-10-27
000136119 264_1 $$2Crossref$$3print$$bInforma UK Limited$$c2010-10-01
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000136119 520__ $$aMitochondrial dysfunction is an early sign of many neurodegenerative diseases. Very recently, two Parkinson disease (PD) associated genes, PINK1 and Parkin, were shown to mediate the degradation of damaged mitochondria via selective autophagy (mitophagy). PINK1 kinase activity is needed for prompt and efficient Parkin recruitment to impaired mitochondria. PD-associated Parkin mutations interfere with the process of mitophagy at distinct steps. Here we show that whole mitochondria are turned over via macroautophagy. Moreover, disease-associated PINK1 mutations also compromise the selective degradation of depolarized mitochondria. This may be due to the decreased physical binding activity of PD-linked PINK1 mutations to Parkin. Thus, PINK1 mutations abrogate autophagy of impaired mitochondria upstream of Parkin. In addition to compromised PINK1 kinase activity, reduced binding of PINK1 to Parkin leads to failure in Parkin mitochondrial translocation, resulting in the accumulation of damaged mitochondria, which may contribute to disease pathogenesis.
000136119 536__ $$0G:(DE-HGF)POF3-345$$a345 - Population Studies and Genetics (POF3-345)$$cPOF3-345$$fPOF III$$x0
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000136119 650_7 $$2NLM Chemicals$$aRNA, Small Interfering
000136119 650_7 $$0EC 2.3.2.27$$2NLM Chemicals$$aUbiquitin-Protein Ligases
000136119 650_7 $$0EC 2.3.2.27$$2NLM Chemicals$$aparkin protein
000136119 650_7 $$0EC 2.7.-$$2NLM Chemicals$$aProtein Kinases
000136119 650_7 $$0EC 2.7.11.1$$2NLM Chemicals$$aPTEN-induced putative kinase
000136119 650_2 $$2MeSH$$aAnimals
000136119 650_2 $$2MeSH$$aAutophagy: genetics
000136119 650_2 $$2MeSH$$aHEK293 Cells
000136119 650_2 $$2MeSH$$aHeLa Cells
000136119 650_2 $$2MeSH$$aHumans
000136119 650_2 $$2MeSH$$aMitochondria: pathology
000136119 650_2 $$2MeSH$$aMitochondria: physiology
000136119 650_2 $$2MeSH$$aMutation
000136119 650_2 $$2MeSH$$aParkinson Disease: genetics
000136119 650_2 $$2MeSH$$aParkinson Disease: pathology
000136119 650_2 $$2MeSH$$aParkinson Disease: physiopathology
000136119 650_2 $$2MeSH$$aProtein Kinases: genetics
000136119 650_2 $$2MeSH$$aProtein Kinases: metabolism
000136119 650_2 $$2MeSH$$aRNA, Small Interfering: genetics
000136119 650_2 $$2MeSH$$aRNA, Small Interfering: metabolism
000136119 650_2 $$2MeSH$$aUbiquitin-Protein Ligases: genetics
000136119 650_2 $$2MeSH$$aUbiquitin-Protein Ligases: metabolism
000136119 7001_ $$0P:(DE-HGF)0$$aHolmström, Kira M$$b1
000136119 7001_ $$0P:(DE-HGF)0$$aTreis, Angela$$b2
000136119 7001_ $$0P:(DE-HGF)0$$aSkujat, Diana$$b3
000136119 7001_ $$0P:(DE-HGF)0$$aWeber, Stephanie S$$b4
000136119 7001_ $$0P:(DE-HGF)0$$aFiesel, Fabienne C$$b5
000136119 7001_ $$0P:(DE-2719)2810803$$aKahle, Philipp$$b6$$eCorresponding author$$udzne
000136119 7001_ $$0P:(DE-HGF)0$$aSpringer, Wolfdieter$$b7$$eCorresponding author
000136119 77318 $$2Crossref$$3journal-article$$a10.4161/auto.6.7.13286$$b : Informa UK Limited, 2010-10-01$$n7$$p871-878$$tAutophagy$$v6$$x1554-8627$$y2010
000136119 773__ $$0PERI:(DE-600)2262043-6$$a10.4161/auto.6.7.13286$$gVol. 6, no. 7, p. 871 - 878$$n7$$p871-878$$q6:7<871 - 878$$tAutophagy$$v6$$x1554-8627$$y2010
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000136119 9141_ $$y2010
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