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Published 24 November 2003. doi:10.1083/jcb.200304046
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© The Rockefeller University Press, 0021-9525/2003/11/701 $8.00
The Journal of Cell Biology, Volume 163, Number 4, 701-706

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 The Drosophila nucleoporin DNup88 localizes DNup214 and CRM1 on the nuclear envelope and attenuates NES-mediated nuclear export

Peggy Roth1, Nikos Xylourgidis1, Nafiseh Sabri1, Anne Uv2, Maarten Fornerod3 and Christos Samakovlis1

1 Department of Developmental Biology, Wenner-Gren Institute, Stockholm University, S-10691 Stockholm, Sweden
2 Department of Medical Biochemistry, Göteborg University, 40530 Göteborg, Sweden
3 Netherlands Cancer Institute H4, 1066 CX Amsterdam, Netherlands

Address correspondence to Christos Samakovlis, Dept. of Developmental Biology, Wenner-Gren Institute, Arrhenius Labs E3, Sv. Arrhenius 16-18, Stockholm University, S-10691 Stockholm, Sweden. Tel.: 46-8-161564. Fax: 46-8- 6126127. email: christos{at}devbio.su.se

Many cellular responses rely on the control of nucleocytoplasmic transport of transcriptional regulators. The Drosophila nucleoporin Nup88 is selectively required for nuclear accumulation of Rel proteins and full activation of the innate immune response. Here, we investigate the mechanisms underlying its role in nucleocytoplasmic transport. Nuclear import of an nuclear localization signal-enhanced green fluorescent protein (NLS-EGFP) reporter is not affected in DNup88 (members only; mbo) mutants, whereas the level of CRM1-dependent EGFP-nuclear export signal (EGFP-NES) export is increased. We show that the nuclear accumulation of the Drosophila Rel protein Dorsal requires CRM1. DNup88 binds to DNup214 and DCRM1 in vitro, and both proteins become mislocalized from the nuclear rim into the nucleus of mbo mutants. Overexpression of DNup88 is sufficient to relocalize DNup214 and CRM1 on the nuclear envelope and revert the mutant phenotypes. We propose that a major function of DNup88 is to anchor DNup214 and CRM1 on the nuclear envelope and thereby attenuate NES-mediated nuclear export.

Key Words: NF{kappa}B; mbo; CAN; NPC; nucleocytoplasmic transport

P. Roth and N. Xylourgidis contributed equally to this paper.

The online version of this article includes supplemental material.

Abbreviations used in this paper: emb, embargoed; LMB, leptomycin B; mbo, members only; NES, nuclear export signal; NPC, nuclear pore complex.


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