The role of NEDD8 Ultimate Buster 1, NUB1, in neurodegenerative α-synucleinopathies

フォーマット:

論文

責任表示:

Tanji, Kunikazu ; Mori, Fumiaki ; Takahashi, Hitoshi ; Kamitani, Tetsu ; Wakabayashi, Koichi

言語:

英語

出版情報:

弘前大学大学院医学研究科・弘前医学会, 2007-11-29

著者名:

• Tanji, Kunikazu
• Mori, Fumiaki
• Takahashi, Hitoshi
• Kamitani, Tetsu
• Wakabayashi, Koichi

掲載情報:

弘前医学

ISSN:

0439-1721      

巻:

59

通号:

Supplement

開始ページ:

S143

終了ページ:

S146

バージョン:

publisher

概要:

NEDD8 is developmentally down-regulated ubiquitin-like protein, which can conjugate covalently to their target proteins. Recently, we identifi ed NUB1 as a NEDD8-interacting protein, which is composed of 601 amino acid residues with a calculated molecular mass of 69.1 kDa. More recently, we showed that NUB1 is an interferon-induced protein and also recruits NEDD8 to the proteasome for degradation. Here, we performed a yeast two-hybrid screening using NUB1 as bait … and isolated the cDNA of synphilin-1 from a human testis cDNA library. Synphilin-1 is a major component of inclusion bodies found in the brains of patients with α-synucleinopathies, including Parkinson’s disease. Our biochemical study showed that NUB1 directly interacts with synphilin-1 through its NEDD8-binding site. In addition, our immunohistochemical study showed that NUB1, as well as synphilin-1, accumulates in the inclusion bodies found in the brains of patients with α-synucleinopathies. These fi ndings imply that NUB1 plays a role in the formation of synphilin-1-positive inclusions. 続きを見る

URL:

http://hdl.handle.net/10129/2228