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J. Biol. Chem., Vol. 278, Issue 23, 20979-20988, June 6, 2003

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Complex Formation among the RNA Export Proteins Nup98, Rae1/Gle2, and TAP^*

Melanie B. Blevins, Ashley M. Smith, Erica M. Phillips and Maureen A. Powers 

From the Department of Cell Biology, Emory University School of Medicine, Atlanta, Georgia 30322

Most nucleocytoplasmic traffic through the nuclear pore complex is mediated by soluble receptors of the importin/exportin or karyopherin family. mRNA export is unique in that no receptor of this family has been implicated in trafficking of the bulk of mRNAs. Instead, many diverse proteins have been linked to mRNA export, but an all-encompassing model remains elusive. Understanding how these proteins interact with each other is central to the development of such a model. Here, we have focused on the interactions between three proteins implicated in mRNA export, Nup98, Rae1/Gle2, and TAP. We have defined the binary complexes that form among these proteins. We find that Gle2 requires two sites within TAP for stable interaction. Strikingly, rather than a general affinity for all nucleoporin FG repeats, TAP has highest affinity for a specific region within the GLFG domain of Nup98, indicating that not all repeats are identical in function. We have established that the ternary complex can form through simultaneous binding of both Gle2 and TAP to adjacent sites on Nup98. In contrast, Nup98 competes with TAP for Gle2 binding; when bound to Nup98, Gle2 no longer interacts directly with TAP. From these interactions, we propose that Gle2 may act to deliver TAP to Nup98 and that this may represent the first in a series of interactions between an export complex and a nucleoporin.

Received for publication, February 27, 2003

^* This work was supported in part by March of Dimes Birth Defects Foundation Basil O'Connor Starter Scholar Research Grant 5-FY98-742 and by National Institutes of Health Grant GM-59975 (to M. A. P.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 404-727-8859; Fax: 404-727-6256; E-mail: mpowers{at}cellbio.emory.edu.

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