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a Department of Biological Regulation and Department of Molecular Cell Biology,
b The Weizmann Institute of Science, Rehovot 76100, Israel
The proteasome engages in protein degradation as a regulatory process in biological transactions. Among other cellular processes, the proteasome participates in degradation of ubiquinated cyclins in mitosis. However, its role in meiosis has not been established. Resumption of meiosis in the oocyte involves the activation of maturation promoting factor (MPF), a complex of p34cdc2 and cyclin B. Inactivation of this factor, occurring between the two meiotic divisions, is associated with degradation of cyclin B. In this study, we examined the possible involvement of the proteasome in regulation of the exit from metaphase I in spontaneously maturing rat oocytes. We found that upon resumption of meiosis, proteasomes translocate to the spindle apparatus. We further demonstrated that specific inhibitors of proteasome catalytic activity, MG132 and lactacystin, blocked polar body extrusion. Chromosome and microtubule fluorescent staining verified that MG132-treated oocytes were arrested at metaphase I. Intervention of proteasomal action with this inhibitor also resulted in accumulation of cyclin B and elevated activity of MPF. These data demonstrate that proteasomal catalytic activity is absolutely essential for the decrease in MPF activity and completion of the first meiotic division. Its translocation to the spindle apparatus may facilitate the timely degradation of cyclin B.
1 This work was partially supported by a grant from the Maria Zondek Hormone Research Fund (N.D.) and the Leo and Julia Forchheimer Center for Molecular Genetics of the Weizmann Institute of Science (A.A.). A.A. is the incumbent of the Joyce and Ben B. Eisenberg professional chair of Molecular Endocrinology and Cancer Research. N.D. is the incumbent of the Phillip M. Klutznick professorial chair of Developmental Biology.
2 Correspondence: FAX: 972 8 9344116; nava.dekel{at}weizmann.ac.il
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