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MeSH Review

Nuclear Pore

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Disease relevance of Nuclear Pore


High impact information on Nuclear Pore

  • Known O-GlcNAcylated proteins include cytoskeletal proteins and their regulatory proteins; viral proteins; nuclear-pore, heat-shock, tumor-suppressor, and nuclearoncogene proteins; RNA polymerase II catalytic subunit; and a multitude of transcription factors [6].
  • Biochemical analyses show that Sus1 interacts with SAGA, a large intranuclear histone acetylase complex involved in transcription initiation, and with the Sac3-Thp1 complex, which functions in mRNA export with specific nuclear pore proteins at the nuclear basket [7].
  • Sus1 is a nuclear protein with a concentration at the nuclear pores [7].
  • Genetic studies, immunolocalization, live imaging, and chromatin immunoprecipitation experiments show that these transport proteins block spreading of heterochromatin by physical tethering of the HML locus to the Nup2p receptor of the nuclear pore complex [8].
  • Transport receptors of the Importin beta family shuttle between the nucleus and cytoplasm and mediate transport of macromolecules through nuclear pore complexes [9].

Chemical compound and disease context of Nuclear Pore

  • These results are consistent with a model in which Rch1 or another member of the karyopherin-alpha family, through the recognition of the MA NLS, participates in docking the HIV-1 nucleoprotein complex at the nuclear pore [10].
  • An Ad2 capsid component, the penton base, expressed as recombinant protein, was found to be capable of affecting the entire entry pathway of adenovirion in HeLa cells, i.e., cell attachment, endocytosis, vesicular escape, intracytoplasmic movement, and translocation through the nuclear pore complex [11].
  • The temporal and spatial changes of intracellular free calcium ([Ca2+]i) within the cytosol and nucleis of C6 glioma cells have been investigated with laser confocal scanning microscopy to evaluate the current view that Ca2+ ions pass freely through nuclear pores by diffusion [12].
  • The numbers of nuclear pore complexes and tight junctions were quantified in the seminal vesicle epithelial cells of castrated and castrated-plus-androgen-treated male rats, which received subcutaneous pellets of testosterone propionate (1 mg/kg body weight) for 1 week [13].
  • This study was aimed at determining whether hyperoxaluria induces the expression of nuclear pore complex oxalate binding protein p62 which has the transport function [14].

Biological context of Nuclear Pore


Anatomical context of Nuclear Pore


Associations of Nuclear Pore with chemical compounds

  • Biochemically altered nuclear pores specifically lacking the N-acetylglucosamine-bearing pore proteins were constructed in a nuclear assembly extract in order to assign function to these proteins [25].
  • NEs incorporating nuclear pores were assembled around beads coated with the guanosine triphosphatase Ran, forming pseudo-nuclei that actively imported nuclear proteins [26].
  • In this study, we show that all of these autoantibodies are directed against a 210-kD integral membrane glycoprotein of the nuclear pore [22].
  • However, the O-linked GlcNAc moieties are only part of the epitopes recognized, since O-GlcNAc-containing limit pronase fragments of nuclear pore complex proteins cannot be immunoprecipitated by these antibodies [27].
  • Immunoferritin labeling of Triton-treated rat liver nuclei demonstrates that gp 190 occurs exclusively in the nuclear pore complex, in the regions of the cytoplasmic (and possibly nucleoplasmic) pore complex annuli [28].

Gene context of Nuclear Pore

  • The NUP1 gene encodes an essential component of the yeast nuclear pore complex [29].
  • Here we show that nuclear-pore-complex extensions formed by the conserved TPR homologues Mlp1 and Mlp2 are responsible for the structural and functional organization of perinuclear chromatin [30].
  • Yra1p interacts directly with the mRNA transport factor Mex67p/Mtr2p, which is associated with the nuclear pore [31].
  • Rip1p is a 42-kD protein associated with nuclear pore complexes and contains nucleoporin-like repeat sequences [32].
  • The export of SSA4 mRNA following stress required functional nuclear pore complexes, as SSA4 mRNA accumulated in nuclei following heat shock of cells containing temperature-sensitive nucleoporins [33].

Analytical, diagnostic and therapeutic context of Nuclear Pore


  1. Autoantibodies from patients with primary biliary cirrhosis preferentially react with the amino-terminal domain of nuclear pore complex glycoprotein gp210. Wesierska-Gadek, J., Hohenauer, H., Hitchman, E., Penner, E. J. Exp. Med. (1995) [Pubmed]
  2. Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Trotman, L.C., Mosberger, N., Fornerod, M., Stidwill, R.P., Greber, U.F. Nat. Cell Biol. (2001) [Pubmed]
  3. Mice lacking the nuclear pore complex protein ALADIN show female infertility but fail to develop a phenotype resembling human triple A syndrome. Huebner, A., Mann, P., Rohde, E., Kaindl, A.M., Witt, M., Verkade, P., Jakubiczka, S., Menschikowski, M., Stoltenburg-Didinger, G., Koehler, K. Mol. Cell. Biol. (2006) [Pubmed]
  4. Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Ojala, P.M., Sodeik, B., Ebersold, M.W., Kutay, U., Helenius, A. Mol. Cell. Biol. (2000) [Pubmed]
  5. Directed inhibition of nuclear import in cellular hypertrophy. Perez-Terzic, C., Gacy, A.M., Bortolon, R., Dzeja, P.P., Puceat, M., Jaconi, M., Prendergast, F.G., Terzic, A. J. Biol. Chem. (2001) [Pubmed]
  6. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Hart, G.W. Annu. Rev. Biochem. (1997) [Pubmed]
  7. Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Rodríguez-Navarro, S., Fischer, T., Luo, M.J., Antúnez, O., Brettschneider, S., Lechner, J., Pérez-Ortín, J.E., Reed, R., Hurt, E. Cell (2004) [Pubmed]
  8. Chromatin boundaries in budding yeast: the nuclear pore connection. Ishii, K., Arib, G., Lin, C., Van Houwe, G., Laemmli, U.K. Cell (2002) [Pubmed]
  9. Structural view of the Ran-Importin beta interaction at 2.3 A resolution. Vetter, I.R., Arndt, A., Kutay, U., Görlich, D., Wittinghofer, A. Cell (1999) [Pubmed]
  10. Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import. Gallay, P., Stitt, V., Mundy, C., Oettinger, M., Trono, D. J. Virol. (1996) [Pubmed]
  11. Cellular uptake and nuclear delivery of recombinant adenovirus penton base. Hong, S.S., Gay, B., Karayan, L., Dabauvalle, M.C., Boulanger, P. Virology (1999) [Pubmed]
  12. Nuclear envelope acts as a calcium barrier in C6 glioma cells. Kong, S.K., Tsang, D., Leung, K.N., Lee, C.Y. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  13. Androgen-induced changes in nuclear pore number and in tight junctions in rat seminal vesicle epithelium. Ortiz, H.E., Cavicchia, J.C. Anat. Rec. (1990) [Pubmed]
  14. Expression of nuclear pore complex oxalate binding protein p62 in experimental hyperoxaluria. Sivakamasundari, P., Sakthivel, R., Kalaiselvi, P., Selvam, R., Varalakshmi, P. Nephron Exp. Nephrol. (2004) [Pubmed]
  15. 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]
  16. RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly. Swaminathan, S., Kiendl, F., Körner, R., Lupetti, R., Hengst, L., Melchior, F. J. Cell Biol. (2004) [Pubmed]
  17. The limited role of NH2-terminal c-Jun phosphorylation in neuronal apoptosis: identification of the nuclear pore complex as a potential target of the JNK pathway. Besirli, C.G., Wagner, E.F., Johnson, E.M. J. Cell Biol. (2005) [Pubmed]
  18. A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1. Wimmer, C., Doye, V., Grandi, P., Nehrbass, U., Hurt, E.C. EMBO J. (1992) [Pubmed]
  19. A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA transport and nuclear pore distribution. Doye, V., Wepf, R., Hurt, E.C. EMBO J. (1994) [Pubmed]
  20. Germ cell-less encodes a cell type-specific nuclear pore-associated protein and functions early in the germ-cell specification pathway of Drosophila. Jongens, T.A., Ackerman, L.D., Swedlow, J.R., Jan, L.Y., Jan, Y.N. Genes Dev. (1994) [Pubmed]
  21. Leucine-rich nuclear-export signals: born to be weak. Kutay, U., Güttinger, S. Trends Cell Biol. (2005) [Pubmed]
  22. The 210-kD nuclear envelope polypeptide recognized by human autoantibodies in primary biliary cirrhosis is the major glycoprotein of the nuclear pore. Courvalin, J.C., Lassoued, K., Bartnik, E., Blobel, G., Wozniak, R.W. J. Clin. Invest. (1990) [Pubmed]
  23. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. Matunis, M.J., Coutavas, E., Blobel, G. J. Cell Biol. (1996) [Pubmed]
  24. Targeting of a cytosolic protein to the nuclear periphery. Hurt, E.C. J. Cell Biol. (1990) [Pubmed]
  25. Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Finlay, D.R., Forbes, D.J. Cell (1990) [Pubmed]
  26. Chromatin-independent nuclear envelope assembly induced by Ran GTPase in Xenopus egg extracts. Zhang, C., Clarke, P.R. Science (2000) [Pubmed]
  27. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. Holt, G.D., Snow, C.M., Senior, A., Haltiwanger, R.S., Gerace, L., Hart, G.W. J. Cell Biol. (1987) [Pubmed]
  28. Identification of a major polypeptide of the nuclear pore complex. Gerace, L., Ottaviano, Y., Kondor-Koch, C. J. Cell Biol. (1982) [Pubmed]
  29. The NUP1 gene encodes an essential component of the yeast nuclear pore complex. Davis, L.I., Fink, G.R. Cell (1990) [Pubmed]
  30. Nuclear pore complexes in the organization of silent telomeric chromatin. Galy, V., Olivo-Marin, J.C., Scherthan, H., Doye, V., Rascalou, N., Nehrbass, U. Nature (2000) [Pubmed]
  31. Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p. Strässer, K., Hurt, E. Nature (2001) [Pubmed]
  32. Yeast heat shock mRNAs are exported through a distinct pathway defined by Rip1p. Saavedra, C.A., Hammell, C.M., Heath, C.V., Cole, C.N. Genes Dev. (1997) [Pubmed]
  33. Regulation of mRNA export in response to stress in Saccharomyces cerevisiae. Saavedra, C., Tung, K.S., Amberg, D.C., Hopper, A.K., Cole, C.N. Genes Dev. (1996) [Pubmed]
  34. Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p. Schmitt, C., von Kobbe, C., Bachi, A., Panté, N., Rodrigues, J.P., Boscheron, C., Rigaut, G., Wilm, M., Séraphin, B., Carmo-Fonseca, M., Izaurralde, E. EMBO J. (1999) [Pubmed]
  35. NUP82 is an essential yeast nucleoporin required for poly(A)+ RNA export. Hurwitz, M.E., Blobel, G. J. Cell Biol. (1995) [Pubmed]
  36. Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96. Grandi, P., Doye, V., Hurt, E.C. EMBO J. (1993) [Pubmed]
  37. The organizational fate of intermediate filament networks in two epithelial cell types during mitosis. Jones, J.C., Goldman, A.E., Yang, H.Y., Goldman, R.D. J. Cell Biol. (1985) [Pubmed]
  38. 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]
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