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

Yukiko Horiike, Hideki Kobayashi, Takeshi Sekiguchi

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)717-723
Number of pages7
JournalMolecular Biology Reports
Volume36
Issue number4
DOIs
Publication statusPublished - Apr 1 2009

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Guanine Nucleotide Exchange Factors
GTP Phosphohydrolases
Serine
Phosphotransferases
Phosphorylation
Electrophoresis, Gel, Two-Dimensional
Threonine
Cricetinae
Karyopherins
Cyclin B
Point Mutation
Glutamic Acid
Cell Survival
Gels
In Vitro Techniques
Growth

All Science Journal Classification (ASJC) codes

  • Genetics
  • Molecular Biology

Cite this

Ran GTPase guanine nucleotide exchange factor RCC1 is phosphorylated on serine 11 by cdc2 kinase in vitro. / Horiike, Yukiko; Kobayashi, Hideki; Sekiguchi, Takeshi.

In: Molecular Biology Reports, Vol. 36, No. 4, 01.04.2009, p. 717-723.

Research output: Contribution to journalArticle

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