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目的:探讨小鼠卵母细胞G2期阻滞中,AKAP7γ是否是介导蛋白激酶A(protein kinaseA,PKA)锚定在Cdc25B底物蛋白处的A型激酶锚定蛋白(A-kinase anchoring proteins,AKAPs)。方法:以PKA锚定阻断剂Ht31处理G2期阻滞的小鼠卵母细胞,观察Cdc25B-S321的磷酸化状态,以免疫共沉淀方法检测PKA RII-AKAP7γ-Cdc25B的相互作用。结果:在G2期阻滞的小鼠卵母细胞中,Ht31处理后Cdc25B-S321不能被PKA磷酸化,同时PKA RII-AKAP7γ及AKAP7γ-Cdc25B存在相互作用。结论:在小鼠卵母细胞中,PKA通过AKAP7γ锚定在胞质中的Cdc25B底物蛋白处,磷酸化其321位丝氨酸,使卵母细胞减数分裂阻滞在G2期,PKA RII-AKAP7γ/Cdc25B通路在小鼠卵母细胞减数分裂阻滞中发挥重要作用。
AIM: To investigate whether AKAP7γ, an inhibitor of protein kinase A (PKA), anchored on the Cdc25B substrate protein during G2 arrest in mouse oocytes, AKAPs). Methods: The mouse oocytes with G2 phase arrest were treated with the PKA-anchored blocker Ht31. The phosphorylation status of Cdc25B-S321 was observed and the interaction of PKA RII-AKAP7γ-Cdc25B was detected by co-immunoprecipitation. Results: Cdc25B-S321 could not be phosphorylated by PKA after Ht31 treatment in mouse G2 oocytes, while PKA RII-AKAP7γ and AKAP7γ-Cdc25B could interact with each other. CONCLUSIONS: In mouse oocytes, PKA is anchored at the Cdc25B substrate protein in the cytoplasm by AKAP7γ, phosphorylating its serine at position 321, causing meiotic arrest of the oocyte at stage G2, PKA RII-AKAP7γ / Cdc25B pathway plays an important role in mouse oocyte meiosis arrest.