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Gene Review

MOG1  -  Mog1p

Saccharomyces cerevisiae S288c

Synonyms: J1827, Multicopy suppressor of GSP1, Nuclear import protein MOG1, YJR074W
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High impact information on MOG1

  • Consistent with the high efficiency of gsp1 suppression, Mog1p directly bound to GTP, but not to GDP-Gsp1p [1].
  • Thus, Mog1p, which was localized in the nucleus, is a Gsp1p-binding protein involved in nuclear-protein import and that functionally interacts with Ntf2p [1].
  • Moreover, MOG1 shows synthetic lethality with PRP20, the Ran guanine nucleotide exchange factor (RanGEF) that also binds nucleotide-free Ran [2].
  • Mog1 is a nuclear protein that interacts with Ran, the Ras family GTPase that confers directionality to nuclear import and export pathways [2].
  • Furthermore, the E65K-Mog1 and K136E-Ran mutations in yeast cause temperature sensitivity and mislocalization of a nuclear import reporter protein, similar to the phenotype observed for the Deltamog1 strain [2].

Biological context of MOG1


Regulatory relationships of MOG1

  • Overexpression of MOG1 is able to suppress temperature-sensitive gsp1 mutants in yeast; Deltamog1 null mutants display temperature-sensitive defects in nuclear trafficking [4].
  • At a concentration corresponding to the molar concentration of GTP-Gsp1p, Yrb1p completely inhibited the Mog1p-stimulated nucleotide release [8].

Other interactions of MOG1

  • A protein required for nuclear-protein import, Mog1p, directly interacts with GTP-Gsp1p, the Saccharomyces cerevisiae ran homologue [1].
  • Yrb1p did not inhibit the Mog1p-stimulated nucleotide release from GTP-Gsp1DeltaC [8].
  • We found that overexpression of Spi1p rescues the S. pombe Delta mog1 cells from death [5].
  • Surprisingly, also unlike the Delta mog1 mutation in S. cerevisiae, the mog1-1 mutation causes nucleolar accumulation of poly(A)(+) RNA at the restrictive temperature in S. pombe, but the signals do not overlap with the fibrillarin-rich region of the nucleolus [5].

Analytical, diagnostic and therapeutic context of MOG1


  1. 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]
  2. Interaction between Ran and Mog1 is required for efficient nuclear protein import. Baker, R.P., Harreman, M.T., Eccleston, J.F., Corbett, A.H., Stewart, M. J. Biol. Chem. (2001) [Pubmed]
  3. Identification and characterization of the human MOG1 gene. Marfatia, K.A., Harreman, M.T., Fanara, P., Vertino, P.M., Corbett, A.H. Gene (2001) [Pubmed]
  4. Crystallization and preliminary X-ray diffraction analysis of the Saccharomyces cerevisiae ran-binding protein Mog1p. Baker, R.P., Stewart, M. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
  5. Fission yeast Mog1p homologue, which interacts with the small GTPase Ran, is required for mitosis-to-interphase transition and poly(A)(+) RNA metabolism. Tatebayashi, K., Tani, T., Ikeda, H. Genetics (2001) [Pubmed]
  6. XMog1, a nuclear ran-binding protein in Xenopus, is a functional homologue of Schizosaccharomyces pombe mog1p that co-operates with RanBP1 to control generation of Ran-GTP. Nicolás, F.J., Moore, W.J., Zhang, C., Clarke, P.R. J. Cell. Sci. (2001) [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. Yrb1p interaction with the gsp1p C terminus blocks Mog1p stimulation of GTP release from Gsp1p. Oki, M., Nishimoto, T. J. Biol. Chem. (2000) [Pubmed]
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