| First Author | Meng J | Year | 2013 |
| Journal | PLoS One | Volume | 8 |
| Issue | 1 | Pages | e53633 |
| PubMed ID | 23326474 | Mgi Jnum | J:231360 |
| Mgi Id | MGI:5770343 | Doi | 10.1371/journal.pone.0053633 |
| Citation | Meng J, et al. (2013) The role of 14-3-3epsilon interaction with phosphorylated Cdc25B at its Ser321 in the release of the mouse oocyte from prophase I arrest. PLoS One 8(1):e53633 |
| abstractText | The protein kinase A (PKA)/Cdc25B pathway plays a critical role in maintaining meiotic arrest in mouse oocytes. However, the molecular mechanism underlying this interchange is not known. In this study, we assessed the role of 14-3-3epsilon interaction with phosphorylated Cdc25B at its Ser321 as the mouse oocyte is released from prophase I arrest. The 14-3-3epsilon isoform is a highly conserved protein with various regulatory roles, including maintenance of meiotic arrest. Cdc25B phosphatase is also a key cell cycle regulator. 14-3-3epsilon binds to Cdc25B-WT, which was abrogated when Ser321 of Cdc25B was mutated to Ala. In addition, we found that 14-3-3epsilon and Cdc25B were co-localized. Cdc25B was translocated from the cytoplasm to the nucleus shortly before germinal vesicle breakdown (GVBD) during the primary oocyte stage of oogenesis. However, mutation of Ser321 to Ala completely abolished the cytoplasmic localization of Cdc25B. Furthermore, oocytes co-expressing of Cdc25B-WT or Cdc25B-Ser321D and 14-3-3epsilon were unable to undergo GVBD. In contrast, co-expression of 14-3-3epsilon and Cdc25B-Ser321A induced GVBD and allowed the process to continue. Down-regulation of 14-3-3epsilon caused partial meiotic resumption. Taken together, these data indicate that Ser321 of Cdc25B is the specific binding site for 14-3-3epsilon binding, and that 14-3-3epsilon is the significant factor in Cdc25B regulation during meiotic resumption of GV stage. |
