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Gene Review

NUP82  -  Nup82p

Saccharomyces cerevisiae S288c

Synonyms: HRB187, J1135, Nuclear pore protein NUP82, Nucleoporin NUP82, YJL061W
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High impact information on NUP82


Biological context of NUP82

  • They do, however, accumulate poly(A)+ RNA in their nuclei at 37 degrees C. We propose that NUP82 acts as a linker to tether nucleoporins directly involved in nuclear transport to pore scaffolding via its coiled-coil domain [5].

Physical interactions of NUP82

  • This suggests that Nup82p may act as a docking site for a core complex composed of the repeat-containing nucleoporins Nup159p and Nsp1p [6].
  • Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p [7].

Other interactions of NUP82

  • The Nup82 protein can be divided into at least two different domains both required for the essential function, but it is only the carboxy-terminal domain, exhibiting heptad repeats, which binds to Nsp1p [4].
  • Together our data suggest that the poly(A)+ RNA export defect previously observed in nup82 mutant cells might be due to the loss from the NPCs of the repeat-containing nucleoporin Nup159p [6].
  • Using a synthetic lethal screen with the nucleoporin NUP1, we have identified a conditional allele of NUP82, encoding an essential nuclear pore complex protein in Saccharomyces cerevisiae [8].
  • Finally, synthetic lethal interactions were found between mutant alleles of NUP116 and all members of the Nup82p complex [9].
  • We show here that overexpression of Rss1/Gle1 also partially rescued depletion of Nup82 [10].

Analytical, diagnostic and therapeutic context of NUP82


  1. Nuclear export of the small ribosomal subunit requires the ran-GTPase cycle and certain nucleoporins. Moy, T.I., Silver, P.A. Genes Dev. (1999) [Pubmed]
  2. Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex. Gleizes, P.E., Noaillac-Depeyre, J., Léger-Silvestre, I., Teulières, F., Dauxois, J.Y., Pommet, D., Azum-Gelade, M.C., Gas, N. J. Cell Biol. (2001) [Pubmed]
  3. In vivo nuclear transport kinetics in Saccharomyces cerevisiae: a role for heat shock protein 70 during targeting and translocation. Shulga, N., Roberts, P., Gu, Z., Spitz, L., Tabb, M.M., Nomura, M., Goldfarb, D.S. J. Cell Biol. (1996) [Pubmed]
  4. A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p. Grandi, P., Emig, S., Weise, C., Hucho, F., Pohl, T., Hurt, E.C. J. Cell Biol. (1995) [Pubmed]
  5. NUP82 is an essential yeast nucleoporin required for poly(A)+ RNA export. Hurwitz, M.E., Blobel, G. J. Cell Biol. (1995) [Pubmed]
  6. Functional characterization of a Nup159p-containing nuclear pore subcomplex. Belgareh, N., Snay-Hodge, C., Pasteau, F., Dagher, S., Cole, C.N., Doye, V. Mol. Biol. Cell (1998) [Pubmed]
  7. Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p. Ho, A.K., Shen, T.X., Ryan, K.J., Kiseleva, E., Levy, M.A., Allen, T.D., Wente, S.R. Mol. Cell. Biol. (2000) [Pubmed]
  8. The karyopherin Msn5/Kap142 requires Nup82 for nuclear export and performs a function distinct from translocation in RPA protein import. Belanger, K.D., Simmons, L.A., Roth, J.K., VanderPloeg, K.A., Lichten, L.B., Fahrenkrog, B. J. Biol. Chem. (2004) [Pubmed]
  9. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. Bailer, S.M., Balduf, C., Katahira, J., Podtelejnikov, A., Rollenhagen, C., Mann, M., Pante, N., Hurt, E. J. Biol. Chem. (2000) [Pubmed]
  10. Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex. Hurwitz, M.E., Strambio-de-Castillia, C., Blobel, G. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
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