Nuclear pore complex function is influenced by glycosylation in Saccharomyces cerevisiae.
Kristy MacDonald, Christina Ott, Laura Davis, Kenneth Belanger
Biology, Colgate University, 13 Oak Dr, Hamilton, NY, 13346, USA
The transport of proteins and RNA between the nucleus and cytoplasm in eukaryotic cells occurs through nuclear pore complexes (NPCs). NPCs are composed of more than 30 different protein subunits, termed nucleoporins (Nups), which are essential for both NPC structure and function. Nup1 is a nucleoporin localized at the nucleoplasmic face of the NPC. nup1 deletion mutants are viable, but grow poorly and have nucleocytoplasmic transport defects at 36oC. In order to identify factors that interact with Nup1 in mediating nuclear transport, we performed a screen for bypass suppressors of nup1 (bnps). We have isolated 35 bnps and have identified one as a deletion of ECM39/ALG12, which encodes an enzyme participating in N-linked glycosylation. Interestingly, we have also observed that nup1 temperature-sensitivity is partially suppressed by incubation in the glycosylation inhibitor tunicamycin. Finally, mutants of POM152, which encodes a glycosylated nucleoporin, are synthetically lethal with nup1. We are currently generating pom152 mutants lacking glycosylated residues and are examining nuclear transport in ecm39 and tunicamycin-treated cells to further characterize the role of glycosylation in NPC function.
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