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Molecular and Cellular Biology, August 2000, p. 5736-5748, Vol. 20, No. 15
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Assembly and Preferential Localization of Nup116p on the Cytoplasmic Face of the Nuclear Pore Complex by Interaction with Nup82p

Albert K. Ho,1 Tian Xiang Shen,1 Kathryn J. Ryan,1 Elena Kiseleva,2,3 Marilyn Aach Levy,1 Terence D. Allen,2 and Susan R. Wente1,*

Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 631101; CRC Department of Structural Cell Biology, Paterson Institute for Cancer Research, Christie Hospital National Health Service Trust, Manchester M20 9BX, United Kingdom2; and Institute of Cytology and Genetics, Russian Academy of Science, Novosibirsk 630090, Russia3

Received 24 January 2000/Returned for modification 27 March 2000/Accepted 9 May 2000

The yeast Saccharomyces cerevisiae nucleoporin Nup116p serves as a docking site for both nuclear import and export factors. However, the mechanism for assembling Nup116p into the nuclear pore complex (NPC) has not been resolved. By conducting a two-hybrid screen with the carboxy (C)-terminal Nup116p region as bait, we identified Nup82p. The predicted coiled-coil region of Nup82p was not required for Nup116p interaction, making the binding requirements distinct from those for the Nsp1p-Nup82p-Nup159p subcomplex (N. Belgareh, C. Snay-Hodge, F. Pasteau, S. Dagher, C. N. Cole, and V. Doye, Mol. Biol. Cell 9:3475-3492, 1998). Immunoprecipitation experiments using yeast cell lysates resulted in the coisolation of a Nup116p-Nup82p subcomplex. Although the absence of Nup116p had no effect on the NPC localization of Nup82p, overexpression of C-terminal Nup116p in a nup116 null mutant resulted in Nup82p mislocalization. Moreover, NPC localization of Nup116p was specifically diminished in a nup82-Delta 108 mutant after growth at 37°C. Immunoelectron microscopy analysis showed Nup116p was localized on both the cytoplasmic and nuclear NPC faces. Its distribution was asymmetric with the majority at the cytoplasmic face. Taken together, these results suggest that Nup82p and Nup116p interact at the cytoplasmic NPC face, with nucleoplasmic Nup116p localization utilizing novel binding partners.

* Corresponding author. Mailing address: Department of Cell Biology & Physiology, Box 8228, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110. Phone: (314) 362-2713. Fax: (314) 747-1259. E-mail: swente{at}cellbio.wustl.edu.

Molecular and Cellular Biology, August 2000, p. 5736-5748, Vol. 20, No. 15
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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