title: Commentary: alpha-synuclein interacts with SOD1 and promotes its oligomerization.
abstract: Alpha-synuclein and Cu, Zn superoxide dismutase (SOD1) are both aggregation-prone proteins that are associated with Parkinson's disease (PD) and amyotrophic lateral sclerosis (ALS), respectively. Recently, we showed that alpha-synuclein interacts with SOD1 in various cell types and tissues. Using a cell culture model, we also found that alpha-synuclein nucleates the polymerization of SOD1. Here, we discuss the current literature regarding their interaction and their co-localization in aggregates of humanpost-mortemtissue. Furthermore we comment on the reported alpha-synuclein-induced SOD1 polymerization in terms of cross-seeding effects in neurodegeneration.
authors.affiliation: Department of Neurology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, Germany.
authors.forename: Anika M
authors.initials: AM
authors.lastname: Helferich
authors.affiliation: Mayo Clinic, Jacksonville, Florida, USA.
authors.forename: Pamela J
authors.initials: PJ
authors.lastname: McLean
authors.affiliation: Department of Neurology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, Germany.
authors.forename: Jochen H
authors.initials: JH
authors.lastname: Weishaupt
authors.affiliation: Department of Neurology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, Germany.
authors.forename: Karin M
authors.initials: KM
authors.lastname: Danzer