14-3-3蛋白结合的靶蛋白包含一个特殊的磷酸化的丝氨酸/苏氨酸结构域，和14-3-3结合能改变他们的催化活性和亚细胞定位。我们通过对小鼠卵母细胞的研究表明，蛋白激酶A(PKA)可直接磷酸化Cdc25的321位丝氨酸，此位点磷酸化后导致14-3-3ε蛋白的结合，Cdc25B活性受抑，卵母细胞发生G2期阻滞。小鼠一细胞期受精卵中是否存在14-3-3ε蛋白以及和cdc25B之间是否存在相互作用，迄今国内外尚未见报道。为了验证14-3-3ε蛋白和Cdc25B蛋白在小鼠一细胞期受精卵G2期阻滞中的作用，本研究以小鼠一细胞期受精卵为研究对象，通过RT-PCR和免疫印迹实验证实确实存在14-3-3ε和Cdc25B蛋白。通过显微共注射14-3-3ε和Cdc25B的mRNA和14-3-3ε的干涉实验探讨14-3-3ε调控一细胞期受精卵G2/M转变的分子机制，为哺乳动物受精卵早期发育的机理研究提供实验依据。

The 14-3-3 proteins bind to target proteins containing specific phospho-serine/theonine motifs, which can in turn alter their catalytic activity or cellular localization .Our recent study demonstrated that PKA can phosphorylate Ser321 of Cdc25B in mouse oocytes. Phosphorylation of Cdc25B on Ser321 creates a binding site for 14-3-3ε adaptor protein, which functionally inactivates Cdc25B by sequestration in the cytoplasm and arrest in G2 phase of meiosis I in mouse oocytes.Little is know about whether exist 14-3-3 protein or which isoforms of 14-3-3 protein exist in mouse one-cell fertilized eggs. To test the role and function of 14-3-3εand Cdc25B protein in G2 arrest of mouse one-cell fertilized eggs. Our previous studies demonstrated that 14-3-3ε and Cdc25B were present in mouse one-cell fertilized eggs (G1,S,G2,M phase) by RT-PCR and Western blotting . Moreover, we construct expressive vector of 14-3-3ε and try to explore the molecular mechanism of G2/M transition of mouse one-cell fertilized eggs by overexpression 14-3-3ε and knockdown of 14-3-3ε. It will be of great importance for the study of mechanisms regulating the fertilized eggs development of human and other mammals.