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Glycogen synthase kinase-3beta phosphorylates synphilin-1 in vitro
Kunikazu Tanji1, Tsutomu Toki, Wakako Tamo
1Department of Neuropathology, Hirosaki University School of Medicine, Hirosaki, Japan.
Abstract:
alpha-Synuclein is known to be a major component of Lewy bodies and glial cytoplasmic inclusions in the brains of patients with alpha-synucleinopathies. Synphilin-1, an alpha-synuclein-associated protein, is also present in these inclusions. However, little is known about the post-translational modifications of synphilin-1. In the present study, it is reported that synphilin-1 is phosphorylated by glycogen synthase kinase-3beta in vitro. It is well known that protein phosphorylation is involved in various physiological phenomena, including signal transduction and protein degradation. Therefore, phosphorylation of synphilin-1 may play an important role in the function of this protein in the brain.