Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1

• Published in: The EMBO journal Vol. 29; no. 20; pp. 3571 - 3589
• Main Authors: Kamp, Frits, Exner, Nicole, Lutz, Anne Kathrin, Wender, Nora, Hegermann, Jan, Brunner, Bettina, Nuscher, Brigitte, Bartels, Tim, Giese, Armin, Beyer, Klaus, Eimer, Stefan, Winklhofer, Konstanze F, Haass, Christian
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 20.10.2010; Nature Publishing Group UK; Nature Publishing Group
• Subjects: alpha-Synuclein - genetics; alpha-Synuclein - metabolism; Animals; Caenorhabditis elegans; Caenorhabditis elegans - cytology; Caenorhabditis elegans - genetics; Caenorhabditis elegans - metabolism; Cell Line; EMBO20; EMBO27; Humans; Immunohistochemistry; Intracellular Signaling Peptides and Proteins - genetics; Intracellular Signaling Peptides and Proteins - metabolism; Membrane Fusion - physiology; mitochondria; Mitochondria - metabolism; Mitochondria - ultrastructure; neurodegeneration; Oncogene Proteins - genetics; Oncogene Proteins - metabolism; Parkinson Disease - metabolism; Parkinson Disease - pathology; Parkinson's disease; Protein Deglycase DJ-1; Protein Kinases - genetics; Protein Kinases - metabolism; Ubiquitin-Protein Ligases - genetics; Ubiquitin-Protein Ligases - metabolism; α-synuclein; neurodegeneration; Parkinson's disease; α‐synuclein; mitochondria

Aggregation of α‐synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD) and a variety of related neurodegenerative disorders. The physiological function of αS is largely unknown. We demonstrate with in vitro vesicle fusion experiments that αS has an inhibitory function on me...