The Mobile FG Nucleoporin Nup98 Is a Cofactor for Crm1-dependent Protein Export

Author:

Oka Masahiro123,Asally Munehiro1,Yasuda Yoshinari1,Ogawa Yutaka1,Tachibana Taro4,Yoneda Yoshihiro123

Affiliation:

1. *Biomolecular Dynamics Group, Graduate School of Frontier Biosciences,

2. Department of Biochemistry, Graduate School of Medicine, Osaka University, and

3. Japan Science and Technology Corporation (JST), Core Research for Evolution Science and Technology (CREST), Osaka University, Suita, Osaka 565-0871, Japan; and

4. Department of Bioengineering, Graduate School of Engineering, Osaka City University, Osaka 558-8585, Japan

Abstract

Nup98 is a mobile nucleoporin that forms distinct dots in the nucleus, and, although a role for Nup98 in nuclear transport has been suggested, its precise function remains unclear. Here, we show that Nup98 plays an important role in Crm1-mediated nuclear protein export. Nuclear, but not cytoplasmic, dots of EGFP-tagged Nup98 disappeared rapidly after cell treatment with leptomycin B, a specific inhibitor of the nuclear export receptor, Crm1. Mutational analysis demonstrated that Nup98 physically and functionally interacts with Crm1 in a RanGTP-dependent manner through its N-terminal phenylalanine-glycine (FG) repeat region. Moreover, the activity of the Nup98-Crm1 complex was modulated by RanBP3, a known cofactor for Crm1-mediated nuclear export. Finally, cytoplasmic microinjection of anti-Nup98 inhibited the Crm1-dependent nuclear export of proteins, concomitant with the accumulation of anti-Nup98 in the nucleus. These results clearly demonstrate that Nup98 functions as a novel shuttling cofactor for Crm1-mediated nuclear export in conjunction with RanBP3.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

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