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Gene Review

NTF2  -  Ntf2p

Saccharomyces cerevisiae S288c

Synonyms: NTF-2, Nuclear transport factor 2, Nuclear transport factor P10, YER009W
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Disease relevance of NTF2


High impact information on NTF2

  • Role of the nuclear transport factor p10 in nuclear import [2].
  • Engineered mutants at the interaction interface reduce the binding of NTF2 to nuclear pores and cause reduced growth rates and Ran mislocalization when substituted for the wild-type protein in yeast [3].
  • The two identical FxFG binding sites on the dimeric molecule are formed by residues from each chain of NTF2 [3].
  • Our data suggest that NTF2 acts at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope [4].
  • We obtained a cDNA encoding NTF2 and showed that the recombinant protein restores transport activity to p62-pretreated cytosol [4].

Biological context of NTF2


Anatomical context of NTF2

  • Previous biochemical studies have shown that NTF2 binds directly to the GDP-bound form of Ran/TC4 and to proteins of the nuclear pore complex that contain phenylalanine-glycine repeats [6].

Associations of NTF2 with chemical compounds

  • Proteins that regulate the GTPase cycle and subcellular distribution of Ran include the cytoplasmic GTPase-activating protein (RanGAP) and its co-factors (RanBP1, RanBP2), the nuclear guanine nucleotide exchange factor (RanGEF), and the Ran import receptor (NTF2) [10].
  • Comparison of the sequences of the xFxFG repeat regions of p62 and Nsplp indicated that NTF2 was probably interacting with the phenylalanine-containing core of these repeats and not the intervening hydrophilic linkers [11].

Physical interactions of NTF2

  • Thus, Mog1p, which was localized in the nucleus, is a Gsp1p-binding protein involved in nuclear-protein import and that functionally interacts with Ntf2p [12].

Other interactions of NTF2

  • Both biochemical and genetic experiments indicate a decreased interaction between Ntf2p, a factor which is required for protein import, and the mutant GSP1 gene products [5].
  • In this study, we report the x-ray crystal structure of the Bre5 NTF2-like domain and show that it forms a homodimeric structure that is similar to other NTF2-like domains, except for the presence of an intermolecular disulfide bond in the crystals [13].
  • Based on these data, we obtained crystals of complexes between yeast NTF2 and a construct containing five FxFG nucleoporin repeats from the yeast nucleoporin Nsp1p and between a construct containing residues 1-442 of human importin-beta and the same nucleoporin construct [14].

Analytical, diagnostic and therapeutic context of NTF2

  • We employed a native gel electrophoresis method to assess the interaction of nucleoporin constructs that contain FxFG sequence repeats with NTF2 and truncation mutants of importin-beta to determine suitable fragments for crystallization [14].


  1. Nuclear protein import is decreased by engineered mutants of nuclear transport factor 2 (NTF2) that do not bind GDP-Ran. Clarkson, W.D., Corbett, A.H., Paschal, B.M., Kent, H.M., McCoy, A.J., Gerace, L., Silver, P.A., Stewart, M. J. Mol. Biol. (1997) [Pubmed]
  2. Role of the nuclear transport factor p10 in nuclear import. Nehrbass, U., Blobel, G. Science (1996) [Pubmed]
  3. Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats. Bayliss, R., Leung, S.W., Baker, R.P., Quimby, B.B., Corbett, A.H., Stewart, M. EMBO J. (2002) [Pubmed]
  4. 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]
  5. Interaction between the small GTPase Ran/Gsp1p and Ntf2p is required for nuclear transport. Wong, D.H., Corbett, A.H., Kent, H.M., Stewart, M., Silver, P.A. Mol. Cell. Biol. (1997) [Pubmed]
  6. High levels of the GTPase Ran/TC4 relieve the requirement for nuclear protein transport factor 2. Paschal, B.M., Fritze, C., Guan, T., Gerace, L. J. Biol. Chem. (1997) [Pubmed]
  7. 1.9 A resolution crystal structure of the Saccharomyces cerevisiae Ran-binding protein Mog1p. Stewart, M., Baker, R.P. J. Mol. Biol. (2000) [Pubmed]
  8. The NTF2 gene encodes an essential, highly conserved protein that functions in nuclear transport in vivo. Corbett, A.H., Silver, P.A. J. Biol. Chem. (1996) [Pubmed]
  9. The interaction between Ran and NTF2 is required for cell cycle progression. Quimby, B.B., Wilson, C.A., Corbett, A.H. Mol. Biol. Cell (2000) [Pubmed]
  10. The mammalian Mog1 protein is a guanine nucleotide release factor for Ran. Steggerda, S.M., Paschal, B.M. J. Biol. Chem. (2000) [Pubmed]
  11. Separate binding sites on nuclear transport factor 2 (NTF2) for GDP-Ran and the phenylalanine-rich repeat regions of nucleoporins p62 and Nsp1p. Clarkson, W.D., Kent, H.M., Stewart, M. J. Mol. Biol. (1996) [Pubmed]
  12. A protein required for nuclear-protein import, Mog1p, directly interacts with GTP-Gsp1p, the Saccharomyces cerevisiae ran homologue. Oki, M., Nishimoto, T. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  13. Structural basis for interaction between the Ubp3 deubiquitinating enzyme and its Bre5 cofactor. Li, K., Zhao, K., Ossareh-Nazari, B., Da, G., Dargemont, C., Marmorstein, R. J. Biol. Chem. (2005) [Pubmed]
  14. Crystallization and initial X-ray diffraction characterization of complexes of FxFG nucleoporin repeats with nuclear transport factors. Bayliss, R., Kent, H.M., Corbett, A.H., Stewart, M. J. Struct. Biol. (2000) [Pubmed]
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