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Journal Article

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

MPS-Authors
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Aksu,  M.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Trakhanov,  S.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Görlich,  D.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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(Supplementary material), 786KB

Citation

Aksu, M., Trakhanov, S., & Görlich, D. (2016). Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. Nature Communications, 7: 11952. doi:10.1038/ncomms11952.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-EA25-E
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.