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Gene Review

NUP159  -  Nup159p

Saccharomyces cerevisiae S288c

Synonyms: NUP158, Nuclear pore protein NUP159, Nucleoporin NUP159, RAT7, YIL115C
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Disease relevance of NUP159


High impact information on NUP159

  • These findings suggest that the Nup159 NTD functions in mRNA export as a binding platform, tethering shuttling Dbp5 molecules at the nuclear periphery and locally concentrating this mRNA remodeling factor at the cytoplasmic face of the NPC [2].
  • The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore [2].
  • Thus, the Nup82p-Nup159p-Nsp1p nucleoporin complex is part of the nuclear export pathways of preribosomes and mRNPs, but with distinct functions in these two processes [3].
  • Examination of nucleoporin mutants reveals that preribosome nuclear export requires the Nup82p-Nup159p-Nsp1p complex [3].
  • Deletion of this portion of Rat7p (Rat7pDeltaN) results in strong defects in mRNA export and eliminates association of Dbp5p with nuclear pores [4].

Biological context of NUP159

  • Its cytoplasmic aspect implies a role for NUP159 in nuclear import [1].
  • Our studies of tRNAs encoded by genes lacking introns show that nucleoporin Nup116p affects both poly(A) RNA and tRNA export, whereas Nup159p affects only poly(A) RNA export [5].

Anatomical context of NUP159


Physical interactions of NUP159

  • Moreover, by in vitro binding assays we showed that Nup82 interacts with the C-terminal region of Nup159, a yeast nucleoporin that previously was also localized to the cytoplasmic side of the NPC [7].

Other interactions of NUP159

  • 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 [8].
  • With Nup42 and Nup159 localized exclusively to the nuclear pore complex cytoplasmic side, we speculated that IP6 may regulate a cytoplasmic step in mRNA export [9].
  • Overexpression of Rss1/Gle1, a putative nucleoporin and/or mRNA transport factor, was shown previously to partially rescue depletion of Nup159 [7].

Analytical, diagnostic and therapeutic context of NUP159

  • Moreover, immunofluorescence analysis demonstrated that Nup159p is delocalized from the NPC in nup82Delta108 cells grown at 37 degrees C, a temperature at which the Nup82Delta108p mutant protein becomes degraded [8].


  1. The essential yeast nucleoporin NUP159 is located on the cytoplasmic side of the nuclear pore complex and serves in karyopherin-mediated binding of transport substrate. Kraemer, D.M., Strambio-de-Castillia, C., Blobel, G., Rout, M.P. J. Biol. Chem. (1995) [Pubmed]
  2. The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore. Weirich, C.S., Erzberger, J.P., Berger, J.M., Weis, K. Mol. Cell (2004) [Pubmed]
  3. 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]
  4. Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells. Hodge, C.A., Colot, H.V., Stafford, P., Cole, C.N. EMBO J. (1999) [Pubmed]
  5. tRNA nuclear export in saccharomyces cerevisiae: in situ hybridization analysis. Sarkar, S., Hopper, A.K. Mol. Biol. Cell (1998) [Pubmed]
  6. 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]
  7. 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]
  8. 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]
  9. Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway. Miller, A.L., Suntharalingam, M., Johnson, S.L., Audhya, A., Emr, S.D., Wente, S.R. J. Biol. Chem. (2004) [Pubmed]
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