Direct association of LIS1, the lissencephaly gene product, with a mammalian homologue of a fungal nuclear distribution protein, rNUDE

FEBS Letters

Arai, Hiroyuki¹  Inoue, Keizo¹  Koizumi, Hiroyuki¹  Kitagawa, Mayumi¹  Umezu, Makiko¹  Aoki, Junken¹ 

[1] Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

关键词: LIS1;    Platelet-activating factor;    Platelet-activating factor acetylhydrolase;    NUDF;    NUDE;    PAF;    platelet-activating factor;    PAF-AH;    platelet-activating factor acetylhydrolase;    nud;    nuclear distribution gene;    rNUDE;    rat NUDE;   

DOI  :  10.1016/S0014-5793(00)01856-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

LIS1 is a product of the causative gene for type I lissencephaly characterized by a smooth brain surface due to a defect in neuronal migration during brain development and a regulatory subunit of platelet-activating factor acetylhydrolase (PAF-AH). It is also a mammalian homologue of the fungal nuclear distribution (nud) gene, nudF, which controls the migration of fungal nuclei. Using the two-hybrid system, we identified a novel LIS1-interacting protein, rat NUDE (rNUDE), and found that it is a mammalian homologue of another fungal nud gene product, NUDE, and Xenopus mitotic phosphoprotein 43 which is phosphorylated in a cell cycle-dependent manner. rNUDE and the catalytic subunits of PAF-AH interact with the N- and C-termini of LIS1, respectively. However, these proteins, instead of simultaneously binding to LIS1, appeared to bind to LIS1 in a competitive manner. These results suggest that LIS1 functions in nuclear migration by interacting with multiple intracellular proteins in mammals.

【 授权许可】

Unknown