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A more recent version of this article appeared on March 1, 2003
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Submitted on August 19, 2002
Revised on October 21, 2002
Accepted on November 18, 2002
1 UMR 7009, CNRS/Université Paris VI, Observatoire Oceanologique de Villefranche sur Mer, 06234, Villefranche sur Mer, France; and School of Biological Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, United Kingdom
2 UMR 7009, CNRS/Université Paris VI, Observatoire Oceanologique de Villefranche sur Mer, 06234, Villefranche sur Mer, France
3 School of Biological Sciences, University of Sussex, Falmer, Brighton, BN1 9QG, United Kingdom
* Corresponding author. E-mail address: beckhel{at}ccrv.obs-vlfr.fr.
We have used complementary biochemical and in vivo approaches to study the compartmentalisation of MPF1 in prophase Xenopus eggs and oocytes. We first examined the distribution of MPF (Cdc2/Cyclin B2) and membranous organelles in high speed extracts of Xenopus eggs made during mitotic prophase. These extracts were found to lack mitochondria, Golgi membranes and most endoplasmic reticulum (ER) but to contain the bulk of the pre-MPF pool. This pre-MPF could be pelleted by further centrifugation along with components necessary to activate it. Upon activation, Cdc2/CyclinB2 moved into the soluble fraction. Electron microscopy and western blot analysis showed that the pre-MPF pellet contained a specific ER subdomain comprising "annulate lamellae" (AL): stacked ER membranes highly enriched in nuclear pores. Co-localisation of pre-MPF with AL was demonstrated by anti-CyclinB2 immunofluorescence in prophase oocytes, in which AL are positioned close to the vegetal surface. GFP-CyclinB2 expressed in oocytes also localised at AL. These data suggest that inactive MPF associates with nuclear envelope components just prior to activation. This association may explain why nuclei and centrosomes stimulate MPF activation and provide a mechanism for targetting of MPF to some of its key substrates.
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