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First published online 10 October 2006
doi: 10.1242/jcs.03201

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The nucleoporin Nup214 sequesters CRM1 at the nuclear rim and modulates NFB activation in Drosophila

Nikos Xylourgidis^*, Peggy Roth^*, Nafiseh Sabri, Vasilios Tsarouhas and Christos Samakovlis

Department of Developmental Biology, Wenner-Gren Institute, Stockholm University, S-10691, Stockholm, Sweden

Author for correspondence (e-mail: christos{at}devbio.su.se)

Accepted 4 August 2006

CRM1-mediated protein export is an important determinant of the nuclear accumulation of many gene regulators. Here, we show that the NFB transcription factor Dorsal is a substrate of CRM1 and requires the nucleoporin Nup214 for its nuclear translocation upon signaling. Nup214 bound to CRM1 directly and anchored it to the nuclear envelope. In nup214 mutants CRM1 accumulated in the nucleus and NES-protein export was enhanced. Nup214 formed complexes with Nup88 and CRM1 in vivo and Nup214 protected Nup88 from degradation at the nuclear rim. In turn, Nup88 was sufficient for targeting the complex to the nuclear pores. Overexpression experiments indicated that Nup214 alone attracts a fraction of CRM1 to the nuclear envelope but does not interfere with NES-GFP export. By contrast, overexpression of the Nup214-Nup88 complex trapped CRM1 and Dorsal to cytoplasmic foci and inhibited protein export and immune response activation. We hypothesize that variation in levels of the Nup214-Nup88 complex at the pore changes the amount of NPC-bound CRM1 and influences the relative strength and duration of NFB signaling responses.

Key words: Drosophila, Nucleoporins, Nup214, CRM1 export, NFB signaling, Nuclear transport

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