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Published online September 17, 2007
doi:10.1083/jcb.200704174
The Journal of Cell Biology, Vol. 178, No. 7, 1121-1132
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Terry et al.
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Article

 Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex

Laura J. Terry and Susan R. Wente

Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232

Correspondence to Susan R. Wente: susan.wente{at}vanderbilt.edu

Trafficking of nucleic acids and large proteins through nuclear pore complexes (NPCs) requires interactions with NPC proteins that harbor FG (phenylalanine-glycine) repeat domains. Specialized transport receptors that recognize cargo and bind FG domains facilitate these interactions. Whether different transport receptors utilize preferential FG domains in intact NPCs is not fully resolved. In this study, we use a large-scale deletion strategy in Saccharomyces cerevisiae to generate a new set of more minimal pore (mmp) mutants that lack specific FG domains. A comparison of messenger RNA (mRNA) export versus protein import reveals unique subsets of mmp mutants with functional defects in specific transport receptors. Thus, multiple functionally independent NPC translocation routes exist for different transport receptors. Our global analysis of the FG domain requirements in mRNA export also finds a requirement for two NPC substructures—one on the nuclear NPC face and one in the NPC central core. These results pinpoint distinct steps in the mRNA export mechanism that regulate NPC translocation efficiency.

Abbreviations used in this paper: cNLS, classic NLS; Kap, karyopherin; MBP, maltose-binding protein; mmp, more minimal pore; mRNP, messenger RNP; NE, nuclear envelope; NES, nuclear export sequence; NLS, nuclear localization signal; NPC, nuclear pore complex; Nup, nucleoporin; SC, synthetic complete.


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