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JCS ePress online publication date 10 Oct 2006
doi: 10.1242/jcs.03201

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jcs.03201v1
119/21/4409    most recent
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Research Article

The nucleoporin Nup214 sequesters CRM1 at the nuclear rim and modulates NF{kappa}B activation in Drosophila


Nikos Xylourgidis, Peggy Roth, Nafiseh Sabri, Vasilios Tsarouhas, and Christos Samakovlis*
* Author for correspondence (e-mail: christos{at}devbio.su.se)

CRM1-mediated protein export is an important determinant of the nuclear accumulation of many gene regulators. Here, we show that the NF{kappa}B 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 NF{kappa}B signaling responses.
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