Figure 4.
Figure 4. Regulation of subcellular localization of Wee1B and Cdc25B. (A) RFP-Cdc25B– or GFP-Wee1B mRNA–injected oocytes were incubated with or without 50 µM roscovitine for 1 h. The arrow indicates a GV oocyte in which Wee1B is exported from the nucleus. (B) Subcellular localization of Ser 321 mutants of Cdc25B. (C) WT or S321A mutant Cdc25B mRNAs were injected into Xenopus oocytes, and the percentage of GVBD was determined after 6 h. The amounts of injected mRNAs were compared by immunoblot analysis. (D) The Ser 321 PKA phosphorylation site is overlapped with the 14-3-3 binding site. Identical and conserved residues are shaded in black and gray, respectively. (E) Immunoprecipitation of Cdc25B mutants and 14-3-3. Black lines indicate that intervening lanes have been spliced out. (F) RFP-Cdc25B was injected into pde3a−/− oocytes and incubated with or without 50 µM H89 for 2 h, and localization of fusion proteins was shown. Bars: (A) 60 µm; (B and F) 20 µm.

Regulation of subcellular localization of Wee1B and Cdc25B. (A) RFP-Cdc25B– or GFP-Wee1B mRNA–injected oocytes were incubated with or without 50 µM roscovitine for 1 h. The arrow indicates a GV oocyte in which Wee1B is exported from the nucleus. (B) Subcellular localization of Ser 321 mutants of Cdc25B. (C) WT or S321A mutant Cdc25B mRNAs were injected into Xenopus oocytes, and the percentage of GVBD was determined after 6 h. The amounts of injected mRNAs were compared by immunoblot analysis. (D) The Ser 321 PKA phosphorylation site is overlapped with the 14-3-3 binding site. Identical and conserved residues are shaded in black and gray, respectively. (E) Immunoprecipitation of Cdc25B mutants and 14-3-3. Black lines indicate that intervening lanes have been spliced out. (F) RFP-Cdc25B was injected into pde3a−/− oocytes and incubated with or without 50 µM H89 for 2 h, and localization of fusion proteins was shown. Bars: (A) 60 µm; (B and F) 20 µm.

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