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Gene Review

NUP62  -  nucleoporin 62kDa

Homo sapiens

Synonyms: 62 kDa nucleoporin, DKFZp547L134, FLJ20822, FLJ43869, IBSN, ...
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Disease relevance of NUP62


Psychiatry related information on NUP62


High impact information on NUP62

  • The relationship between p62 and Sam68, and their roles in Src signalling, need to be clarified, but these findings suggest that Src may participate in regulating RNA processing during the cell cycle [8].
  • Autoantibodies against nucleoporin p62 constitute a novel marker of primary biliary cirrhosis [9].
  • Indeed, we demonstrate that POM121 can recruit several nucleoporins, such as Nup62 or Nup358, to ectopic assembly sites [10].
  • Furthermore, transfection of an antisense construct of p62 severely abrogates NF-kappaB activation [11].
  • Previous studies have shown that immobilized recombinant p62 can bind the cytosolic nuclear import factor NTF2 and thereby deplete transport activity from cytosol [12].

Chemical compound and disease context of NUP62


Biological context of NUP62

  • Isolation involved biochemical complementation of cytosol depleted of this activity by preadsorption with recombinant p62 and the use of a novel flow cytometry-based assay for quantitation of nuclear import [16].
  • However, phosphorylation at Ser-59 (or alternatively, its mutation to Glu) reverses the inhibition and allows interaction of the p56lck SH2 domain with p62 [17].
  • The additional presence of the unique N-terminal region of p56lck prevents p62 binding to the SH2 domain [17].
  • The p56(lck)-interacting protein p62 stimulates transcription via the SV40 enhancer [1].
  • These findings indicate that p62 may link extracellular signals directly to transcriptional responses, and identify the SV40 enhancer as a downstream target for signal transduction pathways in which p62 participates [1].

Anatomical context of NUP62

  • Concomitant with the association of this motor with the NUP62-containing complex is an apparent reorganization of the nuclear pore with loss of NUP62 from larger complexes containing other nucleoporins [18].
  • Using T7-epitope tagged p62 expression in HeLa cells, the expressed protein was shown to bind to the lck SH2 domain [19].
  • Ultrathin sections of Lowicryl K4M embedded cultured 3T3 cells, human keratinocytes and mouse/rat liver tissue were incubated with polyspecific primary antibodies against p62 and other nucleoporins followed by 10 nm gold labeled secondary antibodies [20].
  • We demonstrated physical interaction between HSF2 and p62 both by a glutathione S-transferase (GST) pull-down assay in vitro and by a two-hybrid assay in K562 cells [21].
  • It is suggested that nucleoporin p62 may be targeted and anchored to the pore complex via its carboxy-terminal domain which reveals a hydrophobic heptad repeat organization similar to that found in lamins and other intermediate filament proteins [22].

Associations of NUP62 with chemical compounds


Physical interactions of NUP62

  • Here we describe the association of the KIFC1 motor with a complex containing the nucleoporin NUP62 [18].
  • The trimerization domain of human heat shock factor 2 is able to interact with nucleoporin p62 [21].

Regulatory relationships of NUP62

  • The molecular motor KIFC1 associates with a complex containing nucleoporin NUP62 that is regulated during development and by the small GTPase RAN [18].

Other interactions of NUP62

  • These data suggest the possibility that p62 is involved in the activation or regulation of HSF2 [21].
  • A putative p62-responsive element was localized to the B domain of the distal 72-base pair repeat of the SV40 enhancer. p62 was unable to bind this element in vitro, nor was it able to activate transcription when directly tethered to a promoter, suggesting that p62 stimulates transcription via an indirect mechanism [1].
  • The relocation of cellular proteins and inhibition of nuclear import correlated with the degradation of two NPC components, Nup153 and p62 [24].
  • TAP interacts with multiple components of the NPC including the nucleoporins CAN, Nup98, Nup153, p62, and with three major NPC subcomplexes [25].
  • Expression of the IL4I1 gene from the "NUP62" promoter and the tissue specific involvement of the pre-mRNA processing machinery to regulate expression of two unrelated proteins indicate a novel mechanism of gene regulation [26].

Analytical, diagnostic and therapeutic context of NUP62


  1. The p56(lck)-interacting protein p62 stimulates transcription via the SV40 enhancer. Rachubinski, R.A., Marcus, S.L., Capone, J.P. J. Biol. Chem. (1999) [Pubmed]
  2. Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition. Gustin, K.E., Sarnow, P. EMBO J. (2001) [Pubmed]
  3. RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62. Tantin, D. J. Biol. Chem. (1998) [Pubmed]
  4. A role of the C-terminal part of p44 in the promoter escape activity of transcription factor IIH. Tremeau-Bravard, A., Perez, C., Egly, J.M. J. Biol. Chem. (2001) [Pubmed]
  5. Loss of ubiquitin-binding associated with Paget's disease of bone p62 (SQSTM1) mutations. Cavey, J.R., Ralston, S.H., Hocking, L.J., Sheppard, P.W., Ciani, B., Searle, M.S., Layfield, R. J. Bone Miner. Res. (2005) [Pubmed]
  6. Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation. Kuusisto, E., Salminen, A., Alafuzoff, I. Neuropathol. Appl. Neurobiol. (2002) [Pubmed]
  7. Expression of ubiquitin-binding protein p62 in ubiquitin-immunoreactive intraneuronal inclusions in amyotrophic lateral sclerosis with dementia: analysis of five autopsy cases with broad clinicopathological spectrum. Nakano, T., Nakaso, K., Nakashima, K., Ohama, E. Acta Neuropathol. (2004) [Pubmed]
  8. A mitotic function for Src? Courtneidge, S.A., Fumagalli, S. Trends Cell Biol. (1994) [Pubmed]
  9. Autoantibodies against nucleoporin p62 constitute a novel marker of primary biliary cirrhosis. Wesierska-Gadek, J., Hohenuer, H., Hitchman, E., Penner, E. Gastroenterology (1996) [Pubmed]
  10. Nuclear pore complex assembly and maintenance in POM121- and gp210-deficient cells. Stavru, F., Nautrup-Pedersen, G., Cordes, V.C., Görlich, D. J. Cell Biol. (2006) [Pubmed]
  11. The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. Sanz, L., Sanchez, P., Lallena, M.J., Diaz-Meco, M.T., Moscat, J. EMBO J. (1999) [Pubmed]
  12. Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins. Hu, T., Guan, T., Gerace, L. J. Cell Biol. (1996) [Pubmed]
  13. Viral interactions with the nuclear transport machinery: discovering and disrupting pathways. Fontoura, B.M., Faria, P.A., Nussenzveig, D.R. IUBMB Life (2005) [Pubmed]
  14. Inhibition of sequestosome 1/p62 up-regulation prevents aggregation of ubiquitinated proteins induced by prostaglandin J2 without reducing its neurotoxicity. Wang, Z., Figueiredo-Pereira, M.E. Mol. Cell. Neurosci. (2005) [Pubmed]
  15. An evaluation of sialation of the nucleoporin p62. Fang, B., Hanover, J.A., Miller, M.W. Arch. Biochem. Biophys. (1998) [Pubmed]
  16. Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62. Paschal, B.M., Gerace, L. J. Cell Biol. (1995) [Pubmed]
  17. Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region. Park, I., Chung, J., Walsh, C.T., Yun, Y., Strominger, J.L., Shin, J. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  18. The molecular motor KIFC1 associates with a complex containing nucleoporin NUP62 that is regulated during development and by the small GTPase RAN. Yang, W.X., Jefferson, H., Sperry, A.O. Biol. Reprod. (2006) [Pubmed]
  19. Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain. Joung, I., Strominger, J.L., Shin, J. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  20. Mapping of nucleoporins to the center of the nuclear pore complex by post-embedding immunogold electron microscopy. Grote, M., Kubitscheck, U., Reichelt, R., Peters, R. J. Cell. Sci. (1995) [Pubmed]
  21. The trimerization domain of human heat shock factor 2 is able to interact with nucleoporin p62. Yoshima, T., Yura, T., Yanagi, H. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  22. Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization. Carmo-Fonseca, M., Kern, H., Hurt, E.C. Eur. J. Cell Biol. (1991) [Pubmed]
  23. p62, A TFIIH subunit, directly interacts with thyroid hormone receptor and enhances T3-mediated transcription. Liu, Y., Ando, S., Xia, X., Yao, R., Kim, M., Fondell, J., Yen, P.M. Mol. Endocrinol. (2005) [Pubmed]
  24. Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus. Gustin, K.E., Sarnow, P. J. Virol. (2002) [Pubmed]
  25. The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. Bachi, A., Braun, I.C., Rodrigues, J.P., Panté, N., Ribbeck, K., von Kobbe, C., Kutay, U., Wilm, M., Görlich, D., Carmo-Fonseca, M., Izaurralde, E. RNA (2000) [Pubmed]
  26. Alternative pre-mRNA processing regulates cell-type specific expression of the IL4l1 and NUP62 genes. Wiemann, S., Kolb-Kokocinski, A., Poustka, A. BMC Biol. (2005) [Pubmed]
  27. Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex. Guan, T., Müller, S., Klier, G., Panté, N., Blevitt, J.M., Haner, M., Paschal, B., Aebi, U., Gerace, L. Mol. Biol. Cell (1995) [Pubmed]
  28. Ku70/Ku80 protein complex inhibits the binding of nucleotide excision repair proteins on linear DNA in vitro. Frit, P., Calsou, P., Chen, D.J., Salles, B. J. Mol. Biol. (1998) [Pubmed]
  29. Nuclear pore complex proteins in Alzheimer disease. Sheffield, L.G., Miskiewicz, H.B., Tannenbaum, L.B., Mirra, S.S. J. Neuropathol. Exp. Neurol. (2006) [Pubmed]
  30. A 62-kilodalton tyrosine phosphoprotein constitutively present in primary chronic phase chronic myelogenous leukemia enriched lineage negative blast populations. Wisniewski, D., Strife, A., Wojciechowicz, D., Lambek, C., Clarkson, B. Leukemia (1994) [Pubmed]
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