Emi2 mediates meiotic MII arrest by competitively inhibiting the binding of Ube2S to the APC/C

Kosuke Sako, Kazuhiro Suzuki, Michitaka Isoda, Satomi Yoshikai, Chiharu Senoo, Nobushige Nakajo, Munemichi Ohe and Noriyuki Sagata ()
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Kosuke Sako: Graduate School of Sciences, Kyushu University, Hakozaki 6-10-1
Kazuhiro Suzuki: Graduate School of Sciences, Kyushu University, Hakozaki 6-10-1
Michitaka Isoda: Graduate School of Sciences, Kyushu University, Hakozaki 6-10-1
Satomi Yoshikai: Graduate School of Sciences, Kyushu University, Hakozaki 6-10-1
Chiharu Senoo: Graduate School of Sciences, Kyushu University, Hakozaki 6-10-1
Nobushige Nakajo: Graduate School of Sciences, Kyushu University, Hakozaki 6-10-1
Munemichi Ohe: Graduate School of Sciences, Kyushu University, Hakozaki 6-10-1
Noriyuki Sagata: Graduate School of Sciences, Kyushu University, Hakozaki 6-10-1

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract In vertebrates, unfertilized eggs are arrested at metaphase of meiosis II by Emi2, a direct inhibitor of the APC/C ubiquitin ligase. Two different ubiquitin-conjugating enzymes, UbcH10 and Ube2S, work with the APC/C to target APC/C substrates for degradation. However, their possible roles and regulations in unfertilized/fertilized eggs are not known. Here we use Xenopus egg extracts to show that both UbcH10 and Ube2S are required for rapid cyclin B degradation at fertilization, when APC/C binding of Ube2S, but not of UbcH10, increases several fold, coincidently with (SCFβ-TrCP-dependent) Emi2 degradation. Interestingly, before fertilization, Emi2 directly inhibits APC/C–Ube2S binding via the C-terminal tail, but on fertilization, its degradation allows the binding mediated by the Ube2S C-terminal tail. Significantly, Emi2 and Ube2S bind commonly to the APC/C catalytic subunit APC10 via their similar C-terminal tails. Thus, Emi2 competitively inhibits APC/C–Ube2S binding before fertilization, while its degradation on fertilization relieves the inhibition for APC/C activation.

Date: 2014
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DOI: 10.1038/ncomms4667

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