Regulation of MBK-2/Dyrk kinase by dynamic cortical anchoring during the oocyte-to-zygote transition.

BACKGROUND

Successful transition from oocyte to zygote depends on the timely degradation of oocyte proteins to prepare for embryonic development. In C. elegans, degradation of the oocyte protein MEI-1 depends on MBK-2, a kinase that phosphorylates MEI-1 shortly after fertilization during the second meiotic division.

RESULTS

Here we report that precise timing of MEI-1 phosphorylation depends on the cell cycle-regulated release of MBK-2 from the cortex. Prior to the meiotic divisions, MBK-2 is tethered at the cortex by EGG-3, an oocyte protein required for egg activation (see [1], accompanying paper in this issue). During the meiotic divisions, EGG-3 is internalized and degraded in an APC/C (anaphase-promoting complex/cyclosome)-dependent manner. EGG-3 internalization and degradation correlate with MBK-2 release from the cortex and MEI-1 phosphorylation in the cytoplasm. In an egg-3 mutant, MEI-1 is phosphorylated and degraded prematurely.

CONCLUSION

We suggest that successful transition from an oocyte to a zygote depends on the cell cycle-regulated relocalization of key regulators from the cortex to the cytoplasm of the egg.