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Vol. 12, Issue 9, 2660-2671, September 2001
Centre de Recherche de Biochimie Macromoléculaire, Centre
National de la Recherche Scientifique Unité Propre de Recherche
1086, 34293 Montpellier cedex 5, France
The c-Mos proto-oncogene product plays an essential role during
meiotic divisions in vertebrate eggs. In Xenopus, it is
required for progression of oocyte maturation and meiotic arrest of
unfertilized eggs. Its degradation after fertilization is essential to
early embryogenesis. In this study we investigated the mechanisms
involved in c-Mos degradation. We present in vivo evidence for
ubiquitin-dependent degradation of c-Mos in activated eggs. We found
that c-Mos degradation is not directly dependent on the
anaphase-promoting factor activator Fizzy/cdc20 but requires cyclin
degradation. We demonstrate that cyclin B/cdc2 controls in vivo c-Mos
phosphorylation and stabilization. Moreover, we show that cyclin B/cdc2
is capable of directly phosphorylating c-Mos in vitro, inducing a
similar mobility shift to the one observed in vivo. Tryptic
phosphopeptide analysis revealed a practically identical in vivo and in
vitro phosphopeptide map and allowed identification of serine-3 as the
largely preferential phosphorylation site as previously described
(Freeman et al., 1992). Altogether, these results
demonstrate that, in vivo, stability of c-Mos is directly regulated by cyclin B/cdc2 kinase activity.
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