PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with US-15kD/dim1p via the carboxyl-terminal domain

被引：73

作者：

Waragai, M

Junn, E

Kajikawa, M

Takeuchi, S

Kanazawa, I

Shibata, M

Mouradian, MM

Okazawa, H

机构：

[1] Univ Tokyo, Grad Sch Med, Dept Neurol, Bunkyo Ku, Tokyo 1138655, Japan

[2] NINDS, Expt Therapeut Branch, NIH, Bethesda, MD 20892 USA

[3] Med & Biol Labs Co Ltd, Dept Pharmaceut Dev, Nagano 3960002, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 273卷 / 02期

关键词：

D O I：

10.1006/bbrc.2000.2992

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

PQBP-1 was identified as a binding protein to the polyglutamine tract present in various transcription-related factors and causative genes for neurodegenerative disorders. This novel gene contains at least two functional domains, WW domain and carboxyl-terminal domain (CTD), strictly conserved beyond species. Although human PQBP-1 additionally contains the polar amino acid-rich domain by which it binds to the polyglutamine tract, genuine physiological function(s) have not been clarified. In this study, we showed that U5-15kD, human homologue of fission yeast dim1p, is a partner molecule of PQBP-1 binding to CTD. This finding suggests physiological functions of PQBP-1 in splicing, cell cycle, and ubiquitination, through which we can speculate the pathological roles of PQBP-1 in triplet repeat diseases. (C) 2000 Academic Press.

引用

页码：592 / 595

页数：4

共 14 条

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