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Vol. 10, Issue 3, 649-664, March 1999
and
Department of Biology, University of California at San Diego, La
Jolla, California 92093-0347
The fundamental process of nucleocytoplasmic transport takes place
through the nuclear pore. Peripheral pore structures are presumably
poised to interact with transport receptors and their cargo as these
receptor complexes first encounter the pore. One such peripheral
structure likely to play an important role in nuclear export is the
basket structure located on the nuclear side of the pore. At present,
Nup153 is the only nucleoporin known to localize to the surface of this
basket, suggesting that Nup153 is potentially one of the first pore
components an RNA or protein encounters during export. In this study,
anti-Nup153 antibodies were used to probe the role of Nup153 in nuclear
export in Xenopus oocytes. We found that Nup153
antibodies block three major classes of RNA export, that of
snRNA, mRNA, and 5S rRNA. Nup153 antibodies also block the NES
protein export pathway, specifically the export of the HIV Rev protein,
as well as Rev-dependent RNA export. Not all export was blocked; Nup153
antibodies did not impede the export of tRNA or the recycling of
importin 
to the cytoplasm. The specific antibodies used here also
did not affect nuclear import, whether mediated by importin 
/ or
by transportin. Overall, the results indicate that Nup153 is crucial to
multiple classes of RNA and protein export, being involved at a vital
juncture point in their export pathways. This juncture point appears to
be one that is bypassed by tRNA during its export. We asked whether a
physical interaction between RNA and Nup153 could be observed, using
homoribopolymers as sequence-independent probes for interaction.
Nup153, unlike four other nucleoporins including Nup98, associated
strongly with poly(G) and significantly with poly(U). Thus, Nup153 is
unique among the nucleoporins tested in its ability to interact with RNA and must do so either directly or indirectly through an adaptor protein. These results suggest a unique mechanistic role for Nup153 in
the export of multiple cargos.
Department of Oncological
Sciences, Huntsman Cancer Institute, University of Utah, Salt Lake
City, UT 84108;
Department of Cell Biology, Emory
University, Atlanta, GA 30322.
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