TY - JOUR
T1 - Regulation of MBK-2/Dyrk Kinase by Dynamic Cortical Anchoring during the Oocyte-to-Zygote Transition
AU - Stitzel, Michael L.
AU - Cheng, Ken Chih Chien
AU - Seydoux, Geraldine
N1 - Funding Information:
We thank R. Maruyama and A. Singson for sharing unpublished results and for comments on the manuscript, and S. Mitani and the National Bioresource Project of Japan for egg-3(tm1191). This work was supported by NIH grant HD37047. G.S. is an investigator of the Howard Hughes Medical Institute.
PY - 2007/9/18
Y1 - 2007/9/18
N2 - 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.
AB - 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.
KW - DEVBIO
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U2 - 10.1016/j.cub.2007.08.049
DO - 10.1016/j.cub.2007.08.049
M3 - Article
C2 - 17869113
AN - SCOPUS:34548480470
SN - 0960-9822
VL - 17
SP - 1545
EP - 1554
JO - Current Biology
JF - Current Biology
IS - 18
ER -