The metaphase II arrest in mouse oocytes is controlled through microtubule-dependent destruction of cyclin B in the presence of CSF.
In unfertilized eggs from vertebrates, the cell cycle is arrested in metaphase of the second meiotic division (metaphase II) until fertilization or activation. Maintenance of the long-term meiotic metaphase arrest requires mechanisms preventing the destruction of the maturation promoting factor (MPF) and the migration of the chromosomes. In frog oocytes, arrest in metaphase II (M II) is achieved by cytostatic factor (CSF) that stabilizes MPF, a heterodimer formed of cdc2 kinase and cyclin. At the metaphase/anaphase transition, a rapid proteolysis of cyclin is associated with MPF inactivation. In Drosophila, oocytes are arrested in metaphase I (M I); however, only mechanical forces generated by the chiasmata seem to prevent chromosome separation. Thus, entirely different mechanisms may be involved in the meiotic arrests in various species. We report here that in mouse oocytes a CSF-like activity is involved in the M II arrest (as observed in hybrids composed of fragments of metaphase II-arrested oocytes and activated mitotic mouse oocytes) and that the high activity of MPF is maintained through a continuous equilibrium between cyclin B synthesis and degradation. In addition, the presence of an intact metaphase spindle is required for cyclin B degradation. Finally, MPF activity is preferentially associated with the spindle after bisection of the oocyte. Taken together, these observations suggest that the mechanism maintaining the metaphase arrest in mouse oocytes involves an equilibrium between cyclin synthesis and degradation, probably controlled by CSF, and which is also dependent upon the three-dimensional organization of the spindle.
Kubiak
J Z
JZ
Département de Biologie du Développement, CNRS, Université Paris VII, France.
Weber
M
M
de Pennart
H
H
Winston
N J
NJ
Maro
B
B
D000818:Animals; D002478:Cells, Cultured; D016213:Cyclins / Q000378:metabolism*; D005260:Female; D000090204:Mesothelin; D008677:Metaphase; D051379:Mice; D008870:Microtubules / Q000502:physiology*; D015739:Nocodazole / Q000494:pharmacology; D009865:Oocytes / Q000166:cytology* / Q000187:drug effects / Q000378:metabolism; D006656:Protamine Kinase / Q000378:metabolism; D017231:Proto-Oncogene Proteins c-mos / Q000502:physiology*; D011691:Puromycin / Q000494:pharmacology; D008941:Spindle Apparatus / Q000378:metabolism
D016213:Cyclins; C000715528:Msln protein, mouse; D011691:Puromycin; D006656:Protamine Kinase; D017231:Proto-Oncogene Proteins c-mos; D000090204:Mesothelin; D015739:Nocodazole