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Gene Review

NUP116  -  Nup116p

Saccharomyces cerevisiae S288c

Synonyms: NSP116, Nuclear pore protein NUP116/NSP116, Nucleoporin NUP116/NSP116, YM9532.12C, YMR047C
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High impact information on NUP116

  • A stretch of 140 amino acids within Nup145p is conserved in two other yeast nucleoporins, Nup116p and Nup100p, and in an uncharacterized C. elegans protein [1].
  • Cex1p binds tRNA saturably, and associates with the nuclear pore complex by interacting directly with Nup116p [2].
  • Gle2p is anchored at the nuclear envelope (NE) via a short Gle2p-binding motif within Nup116p called GLEBS [3].
  • A nuclear export signal in Kap95p is required for both recycling the import factor and interaction with the nucleoporin GLFG repeat regions of Nup116p and Nup100p [4].
  • In vivo interaction was demonstrated by isolation of Kap95p from yeast nuclear lysates in either protein A-tagged Nup116p or protein A-tagged Nup100p complexes [4].

Biological context of NUP116


Anatomical context of NUP116

  • Nup116p is a member of a family of five yeast nuclear pore complex (NPC) proteins that share an amino terminal region of repetitive tetrapeptide "GLFG" motifs [5].
  • Previous experiments characterized the unique morphological perturbations that occur in a nup116 null mutant: temperature-sensitive formation of nuclear envelope seals over the cytoplasmic face of the NPC (Wente, S. R., and G. Blobel. 1993. J. Cell Biol. 123:275-284) [5].
  • In situ hybridization with poly(dT) probes showed the accumulation of polyadenylated RNA in the nuclei of arrested nup116 delta cells, sometimes in the form of punctate patches at the nuclear periphery [8].
  • Immuno-gold labeling suggested that Nup159p may be attached to the cytoplasmic ring, whereas Nup116p may be associated, partly, with the cytoplasmic filaments [9].

Physical interactions of NUP116

  • Thus, the in vivo function of Gle2p is strictly coupled to the short GLEBS within Nup116p which links this putative mRNA transport factor to the nuclear pores [10].
  • Nup100p and Nup116p can be co-immunoprecipitated from whole-cell extracts with Upf1p, confirming in vitro the interaction identified by the two-hybrid analysis [11].
  • Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p [12].
  • We have additionally shown that a peptide from the N terminus of the nucleoporin Nup145p-C binds Nup116p-C [13].

Regulatory relationships of NUP116

  • In live yeast, mutated Snl1p could not substitute for wild-type Snl1p in suppressing the lethal defect caused by truncation of the Nup116p nuclear pore component [14].

Other interactions of NUP116

  • The amino-terminal half of Nup145p is similar to two previously identified GLFG nucleoporins, Nup116p and Nup100p (Wente, S. R., M. P. Rout, and G. Blobel. 1992. J. Cell Biol. 119:705-723) [6].
  • Gle2p physically associated with Nup116p in vitro, and the interaction required the N-terminal region of Nup116p [15].
  • Decreased levels of NPC-associated Nsp1p and Nup116p were observed [16].
  • Finally, synthetic lethal interactions were found between mutant alleles of NUP116 and all members of the Nup82p complex [17].
  • Three individual members of this family, NUP49, NUP100, and NUP116, have been isolated and then characterized by a combination of molecular genetics and immunolocalization [7].

Analytical, diagnostic and therapeutic context of NUP116


  1. Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif. Fabre, E., Boelens, W.C., Wimmer, C., Mattaj, I.W., Hurt, E.C. Cell (1994) [Pubmed]
  2. Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery. McGuire, A.T., Mangroo, D. EMBO J. (2007) [Pubmed]
  3. RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. Pritchard, C.E., Fornerod, M., Kasper, L.H., van Deursen, J.M. J. Cell Biol. (1999) [Pubmed]
  4. A nuclear export signal in Kap95p is required for both recycling the import factor and interaction with the nucleoporin GLFG repeat regions of Nup116p and Nup100p. Iovine, M.K., Wente, S.R. J. Cell Biol. (1997) [Pubmed]
  5. The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor. Iovine, M.K., Watkins, J.L., Wente, S.R. J. Cell Biol. (1995) [Pubmed]
  6. NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure. Wente, S.R., Blobel, G. J. Cell Biol. (1994) [Pubmed]
  7. A new family of yeast nuclear pore complex proteins. Wente, S.R., Rout, M.P., Blobel, G. J. Cell Biol. (1992) [Pubmed]
  8. A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic. Wente, S.R., Blobel, G. J. Cell Biol. (1993) [Pubmed]
  9. Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments. Kiseleva, E., Allen, T.D., Rutherford, S., Bucci, M., Wente, S.R., Goldberg, M.W. J. Struct. Biol. (2004) [Pubmed]
  10. Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p. Bailer, S.M., Siniossoglou, S., Podtelejnikov, A., Hellwig, A., Mann, M., Hurt, E. EMBO J. (1998) [Pubmed]
  11. Upf1p, a highly conserved protein required for nonsense-mediated mRNA decay, interacts with the nuclear pore proteins Nup100p and Nup116p. Nazarenus, T., Cedarberg, R., Bell, R., Cheatle, J., Forch, A., Haifley, A., Hou, A., Wanja Kebaara, B., Shields, C., Stoysich, K., Taylor, R., Atkin, A.L. Gene (2005) [Pubmed]
  12. 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]
  13. Multiple conformations in the ligand-binding site of the yeast nuclear pore-targeting domain of Nup116p. Robinson, M.A., Park, S., Sun, Z.Y., Silver, P.A., Wagner, G., Hogle, J.M. J. Biol. Chem. (2005) [Pubmed]
  14. Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. Sondermann, H., Ho, A.K., Listenberger, L.L., Siegers, K., Moarefi, I., Wente, S.R., Hartl, F.U., Young, J.C. J. Biol. Chem. (2002) [Pubmed]
  15. The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function. Ho, A.K., Raczniak, G.A., Ives, E.B., Wente, S.R. Mol. Biol. Cell (1998) [Pubmed]
  16. A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly. Bucci, M., Wente, S.R. Mol. Biol. Cell (1998) [Pubmed]
  17. 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]
  18. Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication. Powers, M.A., Macaulay, C., Masiarz, F.R., Forbes, D.J. J. Cell Biol. (1995) [Pubmed]
  19. Deciphering networks of protein interactions at the nuclear pore complex. Allen, N.P., Patel, S.S., Huang, L., Chalkley, R.J., Burlingame, A., Lutzmann, M., Hurt, E.C., Rexach, M. Mol. Cell Proteomics (2002) [Pubmed]
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