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Gene Review

NUP153  -  nucleoporin 153kDa

Homo sapiens

Synonyms: 153 kDa nucleoporin, HNUP153, N153, Nuclear pore complex protein Nup153, Nucleoporin Nup153
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Disease relevance of NUP153

  • Analysis of components of the NPC revealed that two proteins, Nup153 and p62, were proteolyzed during poliovirus infection [1].

High impact information on NUP153

  • This giant protein comprises an amino-terminal 700-residue leucine-rich region, four RanBP1-homologous (refs 9, 10) domains, eight zinc-finger motifs similar to those of NUP153 (refs 11, 12), and a carboxy terminus with high homology to cyclophilin [2].
  • We uncovered direct interactions of Smad2 with the nucleoporins CAN/Nup214 and Nup153 [3].
  • Strikingly, Nup98 and Nup153 each bound the same four large proteins [4].
  • Importin alpha/beta-mediated protein import into the nucleus was strongly reduced in the absence of Nup153, while transportin-mediated import was unaffected [5].
  • The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins [5].

Biological context of NUP153

  • RanGTP-mediated nuclear export of karyopherin alpha involves its interaction with the nucleoporin Nup153 [6].
  • The specificity of this interaction is demonstrated by its sensitivity to Tpr amino acid substitution mutations that abolish Tpr's ability to adhere to the NPC and affect the direct binding of Tpr to Nup153 [7].
  • Substrate binding by the importin alpha.beta complex and the association of the complex with the nucleoporins Nup358/RanBP2 and Nup153 are not affected by phosphatase inhibitors, suggesting that transport inhibition by protein phosphorylation does not involve these steps [8].
  • Four nucleoporins, Nup153, RanBP2, Nup214 and Tpr are cleaved by caspases during apoptosis [9].
  • Nup153 contains separate binding sites for importin alpha/beta, which mediates classical NLS import, and for transportin, which mediates import of different nuclear proteins [10].

Anatomical context of NUP153


Associations of NUP153 with chemical compounds

  • In contrast, ATP depletion, calcium store depletion by EGTA or thapsigargin, and high concentrations of divalent cation (i.e. 2 mM Ca(2+) and 2 mM Mg(2+)) constrain the distribution of the FG-repeats of Nup153 and Nup214 [14].
  • Targeting information for Nup153 resides in the NH2-terminal domain since this region of the molecule can direct an ordinarily cytoplasmic protein, pyruvate kinase, to the nuclear face of the nuclear pore complex [15].
  • Nup153 is a large O-linked glycoprotein that is a component of the basket-like structure that forms the nucleoplasmic face of nuclear pore complexes (NPCs) [16].

Physical interactions of NUP153

  • Neither Nup153 fragment affected binding of the export receptor Crm1 at the nuclear rim [10].
  • We show that Nup96 and Nup107 are core elements of the NPC proper that are essential for NPC assembly and docking of Nup153 and Tpr to the NPC [17].

Regulatory relationships of NUP153


Other interactions of NUP153

  • Interestingly, FG repeat-containing segments derived from the nucleoporins NUP153 and CAN/NUP214 functioned similarly to those from NUP98 [19].
  • The Ets domain accounted for the bulk of the interaction of PU.1 with Nup153 and RanGMPPNP [18].
  • When lamina assembly is prevented using the dominant-negative mutant XlaminB delta 2+, Nup153 does not appear at the nuclear envelope, while other F/GXFG-containing nucleoporins and Nup93 are recruited normally [20].
  • Nup93 and Nup205 are other NPC core elements that are important for long-term maintenance of NPCs but initially dispensable for the anchoring of Nup153 and Tpr [17].
  • As LB, LAP2 and Nup153 are exposed at the inner face of the nuclear envelope and all interact with chromatin, we suggest that their cleavage allows both the detachment of NE from chromatin and the clustering of NPCs in the plane of the membrane, two conserved morphological features of apoptosis observed in this study [21].

Analytical, diagnostic and therapeutic context of NUP153


  1. Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition. Gustin, K.E., Sarnow, P. EMBO J. (2001) [Pubmed]
  2. A giant nucleopore protein that binds Ran/TC4. Yokoyama, N., Hayashi, N., Seki, T., Panté, N., Ohba, T., Nishii, K., Kuma, K., Hayashida, T., Miyata, T., Aebi, U. Nature (1995) [Pubmed]
  3. Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFbeta signaling complexes in the cytoplasm and nucleus. Xu, L., Kang, Y., Cöl, S., Massagué, J. Mol. Cell (2002) [Pubmed]
  4. Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. Vasu, S., Shah, S., Orjalo, A., Park, M., Fischer, W.H., Forbes, D.J. J. Cell Biol. (2001) [Pubmed]
  5. The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins. Walther, T.C., Fornerod, M., Pickersgill, H., Goldberg, M., Allen, T.D., Mattaj, I.W. EMBO J. (2001) [Pubmed]
  6. RanGTP-mediated nuclear export of karyopherin alpha involves its interaction with the nucleoporin Nup153. Moroianu, J., Blobel, G., Radu, A. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  7. Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex. Hase, M.E., Cordes, V.C. Mol. Biol. Cell (2003) [Pubmed]
  8. Phosphorylation of the nuclear transport machinery down-regulates nuclear protein import in vitro. Kehlenbach, R.H., Gerace, L. J. Biol. Chem. (2000) [Pubmed]
  9. Caspases mediate nucleoporin cleavage, but not early redistribution of nuclear transport factors and modulation of nuclear permeability in apoptosis. Ferrando-May, E., Cordes, V., Biller-Ckovric, I., Mirkovic, J., Görlich, D., Nicotera, P. Cell Death Differ. (2001) [Pubmed]
  10. Separate nuclear import pathways converge on the nucleoporin Nup153 and can be dissected with dominant-negative inhibitors. Shah, S., Forbes, D.J. Curr. Biol. (1998) [Pubmed]
  11. Interactions and three-dimensional localization of a group of nuclear pore complex proteins. Panté, N., Bastos, R., McMorrow, I., Burke, B., Aebi, U. J. Cell Biol. (1994) [Pubmed]
  12. Disruption of the FG nucleoporin NUP98 causes selective changes in nuclear pore complex stoichiometry and function. Wu, X., Kasper, L.H., Mantcheva, R.T., Mantchev, G.T., Springett, M.J., van Deursen, J.M. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  13. The nucleoporin nup153 plays a critical role in multiple types of nuclear export. Ullman, K.S., Shah, S., Powers, M.A., Forbes, D.J. Mol. Biol. Cell (1999) [Pubmed]
  14. Changes in nucleoporin domain topology in response to chemical effectors. Paulillo, S.M., Powers, M.A., Ullman, K.S., Fahrenkrog, B. J. Mol. Biol. (2006) [Pubmed]
  15. Targeting and function in mRNA export of nuclear pore complex protein Nup153. Bastos, R., Lin, A., Enarson, M., Burke, B. J. Cell Biol. (1996) [Pubmed]
  16. Amino-terminal sequences that direct nucleoporin nup153 to the inner surface of the nuclear envelope. Enarson, P., Enarson, M., Bastos, R., Burke, B. Chromosoma (1998) [Pubmed]
  17. Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket. Krull, S., Thyberg, J., Björkroth, B., Rackwitz, H.R., Cordes, V.C. Mol. Biol. Cell (2004) [Pubmed]
  18. Carrier-independent nuclear import of the transcription factor PU.1 via RanGTP-stimulated binding to Nup153. Zhong, H., Takeda, A., Nazari, R., Shio, H., Blobel, G., Yaseen, N.R. J. Biol. Chem. (2005) [Pubmed]
  19. CREB binding protein interacts with nucleoporin-specific FG repeats that activate transcription and mediate NUP98-HOXA9 oncogenicity. Kasper, L.H., Brindle, P.K., Schnabel, C.A., Pritchard, C.E., Cleary, M.L., van Deursen, J.M. Mol. Cell. Biol. (1999) [Pubmed]
  20. Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: evidence from cell-free extracts of Xenopus eggs. Smythe, C., Jenkins, H.E., Hutchison, C.J. EMBO J. (2000) [Pubmed]
  21. Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis. Buendia, B., Santa-Maria, A., Courvalin, J.C. J. Cell. Sci. (1999) [Pubmed]
  22. Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr. Shah, S., Tugendreich, S., Forbes, D. J. Cell Biol. (1998) [Pubmed]
  23. Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153. McMorrow, I., Bastos, R., Horton, H., Burke, B. Biochim. Biophys. Acta (1994) [Pubmed]
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