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© The Rockefeller University Press, 0021-9525/1997//241 $5.00
The Journal of Cell Biology, Volume 136, Number 2, , 1997 241-250

Article

The Vertebrate GLFG Nucleoporin, Nup98, Is an Essential Component of Multiple RNA Export Pathways



Maureen A. Powers*, Douglass J. Forbes*, James E. Dahlberg{ddagger}, and Elsebet Lund{ddagger}

* Department of Biology, University of California at San Diego, La Jolla, California 92093-0347; and {ddagger} Department of Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin 53706

The 97-kD O-linked glycoprotein, Nup98, is a component of the Xenopus laevis nuclear pore complex and the only vertebrate GLFG nucleoporin identified (Powers, M.A., C. Macauley, F. Masiarz, and D.J. Forbes. 1995. J. Cell Biol. 128:721–736). We have investigated possible roles of xNup98 in the nucleocytoplasmic transport of proteins and RNAs by analyzing the consequences of injecting monospecific polyclonal antibodies to xNup98 into X. laevis oocytes. We show here that nuclear injection of anti-xNup98 inhibited the export of multiple classes of RNAs, including snRNAs, 5S RNA, large ribosomal RNAs, and mRNA. In contrast, the export of tRNA was unaffected. Injection of antixNup98 into the oocyte cytoplasm had no effect on export of any of the RNAs. Significantly, nuclear injection of anti-xNup98 antibodies did not inhibit import of either karyophilic proteins or snRNPs. This latter result is in agreement with our previous finding that Nup98 is not an essential element of the protein import pathway. Thus, Nup98 plays a role specifically in RNA export from the nucleus, and it appears to be an essential component of multiple RNA export pathways.

Abbreviations used in this paper: AdML, adenovirus major late; CBC, cap binding complex; NES, nuclear export signal; NLS, nuclear localization signal; snRNPs, small nuclear ribonucleoproteins; WGA, wheat germ agglutinin.

This research was funded by grants from the National Institutes of Health to D.J. Forbes (GM 33279) and to J.E. Dahlberg and E. Lund (GM 30220).

Please address all correspondence to Elsebet Lund, Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706. Tel.: 608.262.1359, Fax.: 608.262.8704. E-mail: elund{at}facstaff.wisc.edu


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