有哪些信誉好的足球投注网站mutations in pink1 and parkin impair ubiquitination of mitofusins in human fibroblasts突变pink1人类成纤维细胞和mitofusins帕金影响泛素化.pdfVIP
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mutations in pink1 and parkin impair ubiquitination of mitofusins in human fibroblasts突变pink1人类成纤维细胞和mitofusins帕金影响泛素化
Mutations in PINK1 and Parkin Impair Ubiquitination of Mitofusins in Human Fibroblasts 1. ¨ 1. 1 ¨ 1 2 Aleksandar Rakovic , Anne Grunewald , Jan Kottwitz , Norbert Bruggemann , Peter P. Pramstaller , 1 1 Katja Lohmann , Christine Klein * ¨ ¨ 1 Section of Clinical and Molecular Neurogenetics, Department of Neurology, University of Lubeck, Lubeck, Germany, 2 Institute of Genetic Medicine, European Academy, Bolzano, Italy Abstract PINK1 and Parkin mutations cause recessive Parkinson’s disease (PD). In Drosophila and SH-SY5Y cells, Parkin is recruited by PINK1 to damaged mitochondria, where it ubiquitinates Mitofusins and consequently promotes mitochondrial fission and mitophagy. Here, we investigated the impact of mutations in endogenous PINK1 and Parkin on the ubiquitination of mitochondrial fusion and fission factors and the mitochondrial network structure. Treating control fibroblasts with mitochondrial membrane potential (Dy) inhibitors or H2O2 resulted in ubiquitination of Mfn1/2 but not of OPA1 or Fis1. Ubiquitination of Mitofusins through the PINK1/Parkin pathway was observed within 1 h of treatment. Upon combined inhibition of Dy and the ubiquitin proteasome system (UPS), no ubiquitination of Mitofusins was detected. Regarding morphological changes, we observed a trend towards increased mitochondrial branching in PD patient cells upon mitochondrial stress. For the first time in PD patien
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