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Gene Review

KAP95  -  Kap95p

Saccharomyces cerevisiae S288c

Synonyms: Importin subunit beta-1, Importin-95, Karyopherin subunit beta-1, Karyopherin-95, L8300.15, ...
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High impact information on KAP95

  • Significantly, symmetric deletions caused mild reductions in Kap95-Kap60-mediated import rates, but virtually abolished Kap104 import [1].
  • Surprisingly, we were unable to detect any defects in the Kap95, Kap121, Xpo1, or mRNA transport pathways in cells expressing the mutant FG Nups [2].
  • Importantly, we show that Kap114p, Kap121p, and Kap95 interact directly with both histone NLSs and that RanGTP inhibits this association [3].
  • Perhaps explaining this disparity, we observed an interaction between RPA and Kap95p in a strain lacking Kap142p [4].
  • In contrast, the NES mutation abolished Kap95p interaction with the GLFG repeat regions from the nucleoporins Nup116p and Nup100p [5].

Biological context of KAP95

  • We have determined that recycling of Kap95p requires a nuclear export signal (NES) [5].
  • A high affinity binding site for a Kap95p import complex was mapped to the C terminus of Nup1p, and, surprisingly, deletion of all FG repeats in that region did not eliminate binding of the complex [6].
  • Microsequence analysis showed that the 95-kDa protein was identical with a yeast protein encoded by gene L8300.15 on chromosome XII [7].

Anatomical context of KAP95


Physical interactions of KAP95


Other interactions of KAP95

  • Srp1p, the yeast nuclear localization signal-receptor, also accumulated in the nuclei of the arrested kap95 mutant cells [5].
  • Kap95p (importin beta) is released from this complex by a direct interaction with Gsp1p-GTP [10].
  • Instead, a 36-amino acid truncation of the C terminus of Nup1p reduced its affinity for the Kap95p import complex by 450-fold [6].
  • In order to understand how nuclear transporters traverse the NPC, we constructed functional protein fusions between several members of the yeast importin family, including Pse1p, Sxm1p, Xpo1p, and Kap95p, and the green fluorescent protein (GFP) [11].
  • Whereas Nup53p is directly involved in NLS-mediated protein import by its interaction with the yeast nuclear import receptor Kap95p, it appears not to participate in NES-dependent nuclear export [12].

Analytical, diagnostic and therapeutic context of KAP95


  1. Minimal nuclear pore complexes define FG repeat domains essential for transport. Strawn, L.A., Shen, T., Shulga, N., Goldfarb, D.S., Wente, S.R. Nat. Cell Biol. (2004) [Pubmed]
  2. The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo. Zeitler, B., Weis, K. J. Cell Biol. (2004) [Pubmed]
  3. Nuclear import of histone H2A and H2B is mediated by a network of karyopherins. Mosammaparast, N., Jackson, K.R., Guo, Y., Brame, C.J., Shabanowitz, J., Hunt, D.F., Pemberton, L.F. J. Cell Biol. (2001) [Pubmed]
  4. The karyopherin Kap142p/Msn5p mediates nuclear import and nuclear export of different cargo proteins. Yoshida, K., Blobel, G. J. Cell Biol. (2001) [Pubmed]
  5. A nuclear export signal in Kap95p is required for both recycling the import factor and interaction with the nucleoporin GLFG repeat regions of Nup116p and Nup100p. Iovine, M.K., Wente, S.R. J. Cell Biol. (1997) [Pubmed]
  6. A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex. Pyhtila, B., Rexach, M. J. Biol. Chem. (2003) [Pubmed]
  7. Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes. Enenkel, C., Blobel, G., Rexach, M. J. Biol. Chem. (1995) [Pubmed]
  8. The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor. Iovine, M.K., Watkins, J.L., Wente, S.R. J. Cell Biol. (1995) [Pubmed]
  9. The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex. Strawn, L.A., Shen, T., Wente, S.R. J. Biol. Chem. (2001) [Pubmed]
  10. Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha. Solsbacher, J., Maurer, P., Vogel, F., Schlenstedt, G. Mol. Cell. Biol. (2000) [Pubmed]
  11. Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase. Seedorf, M., Damelin, M., Kahana, J., Taura, T., Silver, P.A. Mol. Cell. Biol. (1999) [Pubmed]
  12. The yeast nucleoporin Nup53p specifically interacts with Nic96p and is directly involved in nuclear protein import. Fahrenkrog, B., Hübner, W., Mandinova, A., Panté, N., Keller, W., Aebi, U. Mol. Biol. Cell (2000) [Pubmed]
  13. The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex. Denning, D., Mykytka, B., Allen, N.P., Huang, L., Al Burlingame, n.u.l.l., Rexach, M. J. Cell Biol. (2001) [Pubmed]
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