Molecular Biology Reports

, Volume 36, Issue 4, pp 717–723

Ran GTPase guanine nucleotide exchange factor RCC1 is phosphorylated on serine 11 by cdc2 kinase in vitro

Authors

  • Yukiko Horiike
    • Department of Molecular BiologyGraduate School of Medical Science, Kyushu University
  • Hideki Kobayashi
    • Department of Molecular BiologyGraduate School of Medical Science, Kyushu University
    • CREST, Japanese Science and Technology Agency
    • Center for Faculty DevelopmentOkayama University
    • Department of Molecular BiologyGraduate School of Medical Science, Kyushu University
    • CREST, Japanese Science and Technology Agency
Article

DOI: 10.1007/s11033-008-9234-3

Cite this article as:
Horiike, Y., Kobayashi, H. & Sekiguchi, T. Mol Biol Rep (2009) 36: 717. doi:10.1007/s11033-008-9234-3

Abstract

RCC1, a guanine nucleotide exchange factor for Ran GTPase, plays essential roles in the growth and viability of mammalian cells. Here, we examined the phosphorylation of specific serine and threonine residues of RCC1 in vivo and showed that RCC1 is indeed phosphorylated. Analysis by two-dimensional (2D) gel electrophoresis suggested that serine 11 (S11) of hamster RCC1 is phosphorylated in vivo. A point mutation of S11 of hamster RCC1 resulted in a decrease in the number of 2D gel spots, indicating a lack of phosphorylation at the mutant residue. S11 phosphorylation in vitro depended on cyclin B-cdc2 kinase. An RCC1 mutant in which all N-terminal serine and threonine residues were substituted with glutamate residues to mimic phosphorylation at these residues showed decreased binding to the karyopherin, KPNA4, compared with wild type RCC1. We conclude that RCC1 undergoes post-translational phosphorylation.

Keywords

CDK/cyclinKaryopherinPhosphorylationRCC1tsBN2

Copyright information

© Springer Science+Business Media B.V. 2008