Abstract
Ran is a multifunctional small GTPase of the Ras superfamily that plays roles in nucleocytoplasmic transport, mitotic spindle assembly and nuclear envelope formation. By screening a Xenopus oocyte cDNA library for Ran-GTP-binding proteins using the two-hybrid system of co-expression in yeast, we identified XMog1, a 20.4 kDa polypeptide related to Mog1p in Saccharomyces cerevisiae and similar gene products in Schizosaccharomyces pombe, Arabidopsis and mammals. We show that cDNAs encoding XMog1 and S. cerevisiae Mog1p rescue the growth defect of S. pombe cells lacking mog1, demonstrating conservation of their functions. In Xenopus somatic cells and transfected mammalian cells, XMog1 is localised to the nucleus. XMog1 alone does not stimulate Ran GTPase activity or nucleotide exchange, but causes nucleotide release from Ran-GTP and forms a complex with nucleotide-free Ran. However, in combination with Ran-binding protein 1 (RanBP1), XMog1 promotes the release of GDP and the selective binding of GTP to Ran. XMog1 and RanBP1 also promote selective GTP loading onto Ran catalysed by the nuclear guanine nucleotide exchange factor, RCC1. We propose that Mog1-related proteins, together with RanBP1, facilitate the generation of Ran-GTP from Ran-GDP in the nucleus.
| Original language | English |
|---|---|
| Pages (from-to) | 3013-3023 |
| Number of pages | 11 |
| Journal | Journal of Cell Science |
| Volume | 114 |
| Issue number | 16 |
| Early online date | 5 Aug 2001 |
| Publication status | Published - 17 Sep 2001 |
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Keywords
- Nucleocytoplasmic transport
- Ran
- RCC1
- Xenopus egg extracts
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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. (Lead / Corresponding author).
In: Journal of Cell Science, Vol. 114, No. 16, 17.09.2001, p. 3013-3023.Research output: Contribution to journal › Article
TY - JOUR
T1 - 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
AU - Nicolás, F. J.
AU - Moore, W. J.
AU - Zhang, C.
AU - Clarke, P. R.
PY - 2001/9/17
Y1 - 2001/9/17
N2 - Ran is a multifunctional small GTPase of the Ras superfamily that plays roles in nucleocytoplasmic transport, mitotic spindle assembly and nuclear envelope formation. By screening a Xenopus oocyte cDNA library for Ran-GTP-binding proteins using the two-hybrid system of co-expression in yeast, we identified XMog1, a 20.4 kDa polypeptide related to Mog1p in Saccharomyces cerevisiae and similar gene products in Schizosaccharomyces pombe, Arabidopsis and mammals. We show that cDNAs encoding XMog1 and S. cerevisiae Mog1p rescue the growth defect of S. pombe cells lacking mog1, demonstrating conservation of their functions. In Xenopus somatic cells and transfected mammalian cells, XMog1 is localised to the nucleus. XMog1 alone does not stimulate Ran GTPase activity or nucleotide exchange, but causes nucleotide release from Ran-GTP and forms a complex with nucleotide-free Ran. However, in combination with Ran-binding protein 1 (RanBP1), XMog1 promotes the release of GDP and the selective binding of GTP to Ran. XMog1 and RanBP1 also promote selective GTP loading onto Ran catalysed by the nuclear guanine nucleotide exchange factor, RCC1. We propose that Mog1-related proteins, together with RanBP1, facilitate the generation of Ran-GTP from Ran-GDP in the nucleus.
AB - Ran is a multifunctional small GTPase of the Ras superfamily that plays roles in nucleocytoplasmic transport, mitotic spindle assembly and nuclear envelope formation. By screening a Xenopus oocyte cDNA library for Ran-GTP-binding proteins using the two-hybrid system of co-expression in yeast, we identified XMog1, a 20.4 kDa polypeptide related to Mog1p in Saccharomyces cerevisiae and similar gene products in Schizosaccharomyces pombe, Arabidopsis and mammals. We show that cDNAs encoding XMog1 and S. cerevisiae Mog1p rescue the growth defect of S. pombe cells lacking mog1, demonstrating conservation of their functions. In Xenopus somatic cells and transfected mammalian cells, XMog1 is localised to the nucleus. XMog1 alone does not stimulate Ran GTPase activity or nucleotide exchange, but causes nucleotide release from Ran-GTP and forms a complex with nucleotide-free Ran. However, in combination with Ran-binding protein 1 (RanBP1), XMog1 promotes the release of GDP and the selective binding of GTP to Ran. XMog1 and RanBP1 also promote selective GTP loading onto Ran catalysed by the nuclear guanine nucleotide exchange factor, RCC1. We propose that Mog1-related proteins, together with RanBP1, facilitate the generation of Ran-GTP from Ran-GDP in the nucleus.
KW - Nucleocytoplasmic transport
KW - Ran
KW - RCC1
KW - Xenopus egg extracts
UR - http://www.scopus.com/inward/record.url?scp=0034851679&partnerID=8YFLogxK
M3 - Article
C2 - 11686304
AN - SCOPUS:0034851679
VL - 114
SP - 3013
EP - 3023
JO - Journal of Cell Science
JF - Journal of Cell Science
SN - 0021-9533
IS - 16
ER -