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Gene Review

Kpna2  -  karyopherin (importin) alpha 2

Mus musculus

Synonyms: 2410044B12Rik, IPOA1, Importin alpha, Importin alpha P1, Importin subunit alpha-1, ...
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Disease relevance of Kpna2

  • To determine the structural basis of the recognition of diverse bipartite NLSs by mammalian importin-alpha, we co-crystallized a non-autoinhibited mouse receptor protein with peptides corresponding to the NLSs from human retinoblastoma protein and Xenopus laevis phosphoprotein N1N2, containing diverse sequences and lengths of the linker [1].

High impact information on Kpna2

  • IGFBP-3 and -5 have carboxyl-terminal basic motifs incorporating heparin-binding and additional basic residues that interact with the cell surface and matrix, the nuclear transporter importin-beta, and other proteins [2].
  • RAG1 appears to have a binary structure, each half containing multiple regions that can act as NLSs, binding sites for the SRP1/Rch1 family, and RNA binding domains [3].
  • Thus, importin-alpha subtype switching has a major impact on cell differentiation through the regulated nuclear import of a specific set of transcription factors [4].
  • In hippocampal neurons, NMDA receptor activation but not depolarization induced importin nuclear translocation [5].
  • These data suggest a model whereby lesion-induced upregulation of axonal importin beta may enable retrograde transport of signals that modulate the regeneration of injured neurons [6].

Biological context of Kpna2


Anatomical context of Kpna2

  • Chronological quantitative analysis of importin beta-immunostained sections from the transgenic mice revealed a statistically significant progressive decrease in the proportion of the anterior horn cells exhibiting a more intense reactivity for these proteins in the nucleus than in the cytoplasm [11].
  • These results provide in vivo evidence that m-importin is involved in nuclear protein import through association with a NLS in the cytoplasm before nuclear pore binding [12].
  • We suggest that Srp1p interacts with multiple components of the cell nucleus that are required for mitosis and discuss its functional similarities to, and differences from Drosophila pendulin [13].
  • This paper describes genes from yeast and mouse with significant sequence similarities to a Drosophila gene that encodes the blood cell tumor suppressor pendulin [13].
  • An in vitro nuclear import assay using permeabilized HeLa cells revealed that rice importin alpha1, in conjunction with other vertebrate transport factors, mediates the nuclear envelope docking of NLS proteins and their subsequent translocation into the nucleus [14].

Associations of Kpna2 with chemical compounds


Physical interactions of Kpna2


Regulatory relationships of Kpna2


Other interactions of Kpna2


Analytical, diagnostic and therapeutic context of Kpna2


  1. Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha. Fontes, M.R., Teh, T., Jans, D., Brinkworth, R.I., Kobe, B. J. Biol. Chem. (2003) [Pubmed]
  2. Cellular actions of the insulin-like growth factor binding proteins. Firth, S.M., Baxter, R.C. Endocr. Rev. (2002) [Pubmed]
  3. Localization, interaction, and RNA binding properties of the V(D)J recombination-activating proteins RAG1 and RAG2. Spanopoulou, E., Cortes, P., Shih, C., Huang, C.M., Silver, D.P., Svec, P., Baltimore, D. Immunity (1995) [Pubmed]
  4. Triggering neural differentiation of ES cells by subtype switching of importin-alpha. Yasuhara, N., Shibazaki, N., Tanaka, S., Nagai, M., Kamikawa, Y., Oe, S., Asally, M., Kamachi, Y., Kondoh, H., Yoneda, Y. Nat. Cell Biol. (2007) [Pubmed]
  5. Synapse to nucleus signaling during long-term synaptic plasticity; a role for the classical active nuclear import pathway. Thompson, K.R., Otis, K.O., Chen, D.Y., Zhao, Y., O'Dell, T.J., Martin, K.C. Neuron (2004) [Pubmed]
  6. Axoplasmic importins enable retrograde injury signaling in lesioned nerve. Hanz, S., Perlson, E., Willis, D., Zheng, J.Q., Massarwa, R., Huerta, J.J., Koltzenburg, M., Kohler, M., van-Minnen, J., Twiss, J.L., Fainzilber, M. Neuron (2003) [Pubmed]
  7. Importin alpha/beta mediates nuclear transport of a mammalian circadian clock component, mCRY2, together with mPER2, through a bipartite nuclear localization signal. Sakakida, Y., Miyamoto, Y., Nagoshi, E., Akashi, M., Nakamura, T.J., Mamine, T., Kasahara, M., Minami, Y., Yoneda, Y., Takumi, T. J. Biol. Chem. (2005) [Pubmed]
  8. A centriole- and RanGTP-independent spindle assembly pathway in meiosis I of vertebrate oocytes. Dumont, J., Petri, S., Pellegrin, F., Terret, M.E., Bohnsack, M.T., Rassinier, P., Georget, V., Kalab, P., Gruss, O.J., Verlhac, M.H. J. Cell Biol. (2007) [Pubmed]
  9. Biophysical characterization of interactions involving importin-alpha during nuclear import. Catimel, B., Teh, T., Fontes, M.R., Jennings, I.G., Jans, D.A., Howlett, G.J., Nice, E.C., Kobe, B. J. Biol. Chem. (2001) [Pubmed]
  10. Genomic organization and chromosomal localization of the importin alpha1 gene in the mouse. Miyamoto, Y., Kim, J., Yuba, S., Yoneda, Y. Gene (2002) [Pubmed]
  11. Altered distributions of nucleocytoplasmic transport-related proteins in the spinal cord of a mouse model of amyotrophic lateral sclerosis. Zhang, J., Ito, H., Wate, R., Ohnishi, S., Nakano, S., Kusaka, H. Acta Neuropathol. (2006) [Pubmed]
  12. In vivo evidence for involvement of a 58 kDa component of nuclear pore-targeting complex in nuclear protein import. Imamoto, N., Shimamoto, T., Takao, T., Tachibana, T., Kose, S., Matsubae, M., Sekimoto, T., Shimonishi, Y., Yoneda, Y. EMBO J. (1995) [Pubmed]
  13. Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis. Küssel, P., Frasch, M. Mol. Gen. Genet. (1995) [Pubmed]
  14. Functional characterization of a plant importin alpha homologue. Nuclear localization signal (NLS)-selective binding and mediation of nuclear import of nls proteins in vitro. Jiang, C.J., Imamoto, N., Matsuki, R., Yoneda, Y., Yamamoto, N. J. Biol. Chem. (1998) [Pubmed]
  15. Nuclear import of the retinoid X receptor, the vitamin D receptor, and their mutual heterodimer. Yasmin, R., Williams, R.M., Xu, M., Noy, N. J. Biol. Chem. (2005) [Pubmed]
  16. Myb-binding protein 1a is a nucleocytoplasmic shuttling protein that utilizes CRM1-dependent and independent nuclear export pathways. Keough, R.A., Macmillan, E.M., Lutwyche, J.K., Gardner, J.M., Tavner, F.J., Jans, D.A., Henderson, B.R., Gonda, T.J. Exp. Cell Res. (2003) [Pubmed]
  17. Crystallization of importin alpha, the nuclear-import receptor. Teh, T., Tiganis, T., Kobe, B. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
  18. Role of prodomain in importin-mediated nuclear localization and activation of caspase-2. Baliga, B.C., Colussi, P.A., Read, S.H., Dias, M.M., Jans, D.A., Kumar, S. J. Biol. Chem. (2003) [Pubmed]
  19. Importin alpha transports CaMKIV to the nucleus without utilizing importin beta. Kotera, I., Sekimoto, T., Miyamoto, Y., Saiwaki, T., Nagoshi, E., Sakagami, H., Kondo, H., Yoneda, Y. EMBO J. (2005) [Pubmed]
  20. Promotion of importin alpha-mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3. Faul, C., Hüttelmaier, S., Oh, J., Hachet, V., Singer, R.H., Mundel, P. J. Cell Biol. (2005) [Pubmed]
  21. The nuclear pore-targeting complex binds to nuclear pores after association with a karyophile. Imamoto, N., Shimamoto, T., Kose, S., Takao, T., Tachibana, T., Matsubae, M., Sekimoto, T., Shimonishi, Y., Yoneda, Y. FEBS Lett. (1995) [Pubmed]
  22. Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling. Matsuura, Y., Stewart, M. EMBO J. (2005) [Pubmed]
  23. Impaired expression of importin/karyopherin beta1 leads to post-implantation lethality. Miura, K., Yoshinobu, K., Imaizumi, T., Haruna, K., Miyamoto, Y., Yoneda, Y., Nakagata, N., Araki, M., Miyakawa, T., Yamamura, K., Araki, K. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  24. Cleavage stage porcine embryos may have differing developmental requirements for karyopherins alpha2 and alpha3. Cabot, R.A., Prather, R.S. Mol. Reprod. Dev. (2003) [Pubmed]
  25. Differential importin-alpha recognition and nuclear transport by nuclear localization signals within the high-mobility-group DNA binding domains of lymphoid enhancer factor 1 and T-cell factor 1. Prieve, M.G., Guttridge, K.L., Munguia, J., Waterman, M.L. Mol. Cell. Biol. (1998) [Pubmed]
  26. Association of the T-cell protein tyrosine phosphatase with nuclear import factor p97. Tiganis, T., Flint, A.J., Adam, S.A., Tonks, N.K. J. Biol. Chem. (1997) [Pubmed]
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