Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A

Metin Aksu, Sergei Trakhanov and Dirk Görlich ()
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Metin Aksu: Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
Sergei Trakhanov: Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
Dirk Görlich: Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: Abstract Xpo4 is a bidirectional nuclear transport receptor that mediates nuclear export of eIF5A and Smad3 as well as import of Sox2 and SRY. How Xpo4 recognizes such a variety of cargoes is as yet unknown. Here we present the crystal structure of the RanGTP·Xpo4·eIF5A export complex at 3.2 Å resolution. Xpo4 has a similar structure as CRM1, but the NES-binding site is occluded, and a new interaction site evolved that recognizes both globular domains of eIF5A. eIF5A contains hypusine, a unique amino acid with two positive charges, which is essential for cell viability and eIF5A function in translation. The hypusine docks into a deep, acidic pocket of Xpo4 and is thus a critical element of eIF5A’s complex export signature. This further suggests that Xpo4 recognizes other cargoes differently, and illustrates how Xpo4 suppresses – in a chaperone-like manner – undesired interactions of eIF5A inside nuclei.

Date: 2016
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DOI: 10.1038/ncomms11952

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