Calcium triggers exit from meiosis II by targeting the APC/C inhibitor XErp1 for degradation

Nadine R. Rauh, Andreas Schmidt, Jenny Bormann, Erich A. Nigg and Thomas U. Mayer ()
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Nadine R. Rauh: Chemical Biology, Independent Research Group
Andreas Schmidt: Chemical Biology, Independent Research Group
Jenny Bormann: Chemical Biology, Independent Research Group
Erich A. Nigg: Max Planck Institute of Biochemistry
Thomas U. Mayer: Chemical Biology, Independent Research Group

Nature, 2005, vol. 437, issue 7061, 1048-1052

Abstract: Abstract Vertebrate eggs awaiting fertilization are arrested at metaphase of meiosis II by a biochemical activity termed cytostatic factor (CSF)1,2. This activity inhibits the anaphase-promoting complex/cyclosome (APC/C), a ubiquitin ligase that triggers anaphase onset and mitotic/meiotic exit by targeting securin and M-phase cyclins for destruction3,4,5. On fertilization a transient rise in free intracellular calcium6 causes release from CSF arrest and thus APC/C activation. Although it has previously been shown that calcium induces the release of APC/C from CSF inhibition through calmodulin-dependent protein kinase II (CaMKII)7,8, the relevant substrates of this kinase have not been identified. Recently, we characterized XErp1 (Emi2), an inhibitor of the APC/C and key component of CSF activity in Xenopus egg extract9. Here we show that calcium-activated CaMKII triggers exit from meiosis II by sensitizing the APC/C inhibitor XErp1 for polo-like kinase 1 (Plx1)-dependent degradation. Phosphorylation of XErp1 by CaMKII leads to the recruitment of Plx1 that in turn triggers the destruction of XErp1 by phosphorylating a site known to serve as a phosphorylation-dependent degradation signal. These results provide a molecular explanation for how the fertilization-induced calcium increase triggers exit from meiosis II.

Date: 2005
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DOI: 10.1038/nature04093

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