HGNC Approved Gene Symbol: NUP153
Cytogenetic location: 6p22.3 Genomic coordinates (GRCh38): 6:17,615,037-17,706,925 (from NCBI)
Nuclear pore complexes are elaborate structures that mediate the regulated movement of macromolecules between the nucleus and cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. Nucleoporins are pore complex-specific glycoproteins characterized by cytoplasmically oriented O-linked N-acetylglucosamine residues and numerous repeats of the pentapeptide sequence XFXFG.
By immunoscreening a HeLa cell cDNA expression library with a monoclonal antibody that recognizes a group of nucleoporins, McMorrow et al. (1994) isolated a cDNA encoding NUP153. The deduced 1,475-amino acid protein has a calculated molecular mass of 153.8 kD. It contains 33 copies of the XFXFG sequence, a C-terminal half that is serine- and threonine-rich, and 4 sequence motifs that resemble those of zinc fingers. The human and rat NUP153 proteins are 82% identical. Northern blot analysis detected a 6-kb human NUP153 mRNA.
Ullman et al. (1999) found that antibodies to Xenopus Nup153 blocked export of snRNA, mRNA, and 5S rRNA from the nucleus, but did not impede export of tRNA or recycling of importin-beta (see KPNB1; 602738) to the cytoplasm. They also determined that Nup153, unlike other nucleoporins, associates strongly with poly(G) and poly(U). The interaction may be direct or may be via an adaptor protein.
By immunogold electron microscopy, Walther et al. (2001) localized Xenopus Nup153 to the nuclear ring of the nuclear pore complex (NPC). NPCs assembled in the absence of Nup153 lacked several nuclear basket components, were unevenly distributed in the nuclear envelope, and, unlike wildtype NPCs, were mobile within the nuclear envelope. Nuclear import events requiring importin-alpha (see KPNA5; 604545)/importin-beta were also defective due to reduced translocation of the import complex rather than defective receptor recycling.
Liu et al. (2003) found that a central region of Xenopus Nup153 associated with COPI (601924), a coatomer complex previously characterized in the context of vesicle budding during trafficking within the Golgi and between the Golgi and the endoplasmic reticulum. Nup153 recruited COPI to the nuclear membrane during mitosis, suggesting that vesiculation is an important step in nuclear envelope breakdown. Perturbing the function of the COPI complex impaired nuclear envelope disassembly.
The International Radiation Hybrid Mapping Consortium mapped the NUP153 gene to chromosome 6 (WI-7306).
Liu, J., Prunuske, A. J., Fager, A. M., Ullman, K. S. The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153. Dev. Cell 5: 487-498, 2003. [PubMed: 12967567] [Full Text: https://doi.org/10.1016/s1534-5807(03)00262-4]
McMorrow, I., Bastos, R., Horton, H., Burke, B. Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153. Biochim. Biophys. Acta 1217: 219-223, 1994. [PubMed: 8110839] [Full Text: https://doi.org/10.1016/0167-4781(94)90040-x]
Ullman, K. S., Shah, S., Powers, M. A., Forbes, D. J. The nucleoporin Nup153 plays a critical role in multiple types of nuclear export. Molec. Biol. Cell 10: 649-664, 1999. [PubMed: 10069809] [Full Text: https://doi.org/10.1091/mbc.10.3.649]
Walther, T. C., Fornerod, M., Pickersgill, H., Goldberg, M., Allen, T. D., Mattaj, I. W. The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins. EMBO J. 20: 5703-5714, 2001. [PubMed: 11598013] [Full Text: https://doi.org/10.1093/emboj/20.20.5703]