Glycogen synthase kinase-3β phosphorylates synphilin-1 in vitro

被引：7

作者：

Tanji, K

Toki, T

Tamo, W

Imaizumi, T

Matsumiya, T

Mori, F

Takahashi, H

Satoh, K

Wakabayashi, K

机构：

[1] Hirosaki Univ, Dept Neuropathol, Inst Brain Sci, Sch Med, Hirosaki, Aomori 0368562, Japan

[2] Hirosaki Univ, Dept Pediat, Inst Brain Sci, Sch Med, Hirosaki, Aomori 0368562, Japan

[3] Hirosaki Univ, Dept Vasc Biol, Inst Brain Sci, Sch Med, Hirosaki, Aomori 0368562, Japan

[4] Hirosaki Univ, Dept Dent & Oral Surg, Sch Med, Hirosaki, Aomori 0368562, Japan

[5] Niigata Univ, Dept Pathol, Brain Res Inst, Niigata, Japan

来源：

NEUROPATHOLOGY | 2003年 / 23卷 / 03期

关键词：

alpha-synuclein; glycogen synthase kinase-3 beta; phosphorylation; synphilin-1;

D O I：

10.1046/j.1440-1789.2003.00503.x

中图分类号：

R74 [神经病学与精神病学];

学科分类号：

摘要：

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 posttranslational 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.

引用

页码：199 / 202

页数：4

共 19 条

[1] Parkin ubiquitinates the α-synuclein-interacting protein, synphilin-1:: implications for Lewy-body formation in Parkinson disease [J].