| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1929327 | Biochemical and Biophysical Research Communications | 2012 | 6 Pages |
α-Synuclein is the major component of Lewy bodies and Lewy neurites, the pathological hallmarks of surviving neuronal cells in Parkinson’s disease patients. However, the physiological role played by α-synuclein remains unclear. In this study, spectrin beta non-erythrocyte 1 (SPTBN1) interacted with α-synuclein in phage display assays using a normalized human brain cDNA library. A direct interaction between α-synuclein and SPTBN1 was confirmed by GST pull-down and co-immunoprecipitation assays. SPTBN1 and α-synuclein proteins colocalized in N2a neuronal cells. Transfection of SPTBN1 caused human SH-SY5Y dopaminergic neuron cells to inappropriately induce neurites, which extended from cell bodies. Cotransfection with α-synuclein reversed SPTBN1-induced excessive neurite branching in SH-SY5Y cells, and only a single neurite extended from each neuron. These results suggest that α-synuclein modulates neurite outgrowth by interacting with cytoskeletal proteins such as SPTBN1.
► SPTBN1 was identified as an α-synuclein-interacting partner in a phage display screen. ► SPTBN1 specifically interacted with α-synuclein in vitro and in neuronal cells. ► Overexpression of SPTBN1 induced excessive neurite formation from dopaminergic neuronal cell bodies. ► Cotransfection with α-synuclein reversed SPTBN1-induced neurite branching. ► α-Synuclein may modulate neurite outgrowth by interacting with the cytoskeletal protein SPTBN1.
