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Residual Cdc2 activity remaining at meiosis I exit is essential for meiotic M-M transition in Xenopus oocyte extracts.
Iwabuchi M
,
Ohsumi K
,
Yamamoto TM
,
Sawada W
,
Kishimoto T
.
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To investigate the regulatory mechanisms of the cell cycle transition from M phase to M phase in meiotic cycles, a Xenopus oocyte extract that performs the M-M transition has been developed. Using the meiotic extract, we found that a low level of Cdc2 activity remained at the exit of meiosis I (MI), due to incomplete degradation of cyclin B. The inactivation of the residual Cdc2 activity induced both entry into S phase and tyrosine phosphorylation on Cdc2 after MI. Quantitative analysis demonstrated that a considerable amount of Wee1 was present at the MI exit and Cdc2 inhibitory phosphorylation during this period was suppressed by the dominance of Cdc2 over Wee1. Consistently, the addition of more than a critical amount of Wee1 to the extract induced Cdc2 inhibitory phosphorylation, changing the M-M transition into an M-S-M transition. Thus, the Cdc2 activity remaining at MI exit is required for suppressing entry into S phase during the meiotic M-M transition period.
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