GLE2 encodes a nuclear pore protein homologous to the nucleoporin Rae1p identified in S. pombe and mammalian cells (5, 1, 6, 7). Transport of macromolecules between the nucleus and the cytoplasm of eukaryotic cells occurs through the nuclear pore complex (NPC), a large macromolecular complex that spans the nuclear envelope (reviewed in 7, 8, 9, 10). The structure of the vertebrate NPC has been studied extensively; recent reviews include 11, 12, 13, and 14. The yeast NPC shares several features with the vertebrate NPC, despite being smaller and less elaborate (15, 16). Many yeast nuclear pore proteins, or nucleoporins, have been identified by a variety of genetic approaches (reviewed in 7, 8, 17, 18, 19). GLE2 was identified by a mutation that is synthetically lethal with a nup100 null mutation (1), and interacts genetically with genes encoding other nucleoporins and nuclear transport factors (20). Gle2p forms a stable complex with the nucleoporin Nup116p (21, 22); binding to Nup116p is required for Gle2p to associate with nuclear pores (22). Gle2p also associates with the nuclear localization signal receptor Srp1p and Nup42p, which interacts with nuclear export signals. Mutations in GLE2 block export of polyadenylated RNA from the nucleus, and cause defects in NPC and nuclear envelope structure (1).

Last updated: 1999-08-05