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-Structure paper
タイトル | Atomic structure of the APC/C and its mechanism of protein ubiquitination. |
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ジャーナル・号・ページ | Nature, Vol. 522, Issue 7557, Page 450-454, Year 2015 |
掲載日 | 2015年6月25日 |
著者 | Leifu Chang / Ziguo Zhang / Jing Yang / Stephen H McLaughlin / David Barford / |
PubMed 要旨 | The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by coactivator subunits, phosphorylation, the ...The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by coactivator subunits, phosphorylation, the mitotic checkpoint complex and interphase early mitotic inhibitor 1 (Emi1) ensures the correct order and timing of distinct cell-cycle transitions. Here we use cryo-electron microscopy to determine atomic structures of APC/C-coactivator complexes with either Emi1 or a UbcH10-ubiquitin conjugate. These structures define the architecture of all APC/C subunits, the position of the catalytic module and explain how Emi1 mediates inhibition of the two E2s UbcH10 and Ube2S. Definition of Cdh1 interactions with the APC/C indicates how they are antagonized by Cdh1 phosphorylation. The structure of the APC/C with UbcH10-ubiquitin reveals insights into the initiating ubiquitination reaction. Our results provide a quantitative framework for the design of future experiments to investigate APC/C functions in vivo. |
リンク | Nature / PubMed:26083744 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 - 7.3 Å |
構造データ | EMDB-2924: Cryo-EM structure of the human APC/C-Cdh1-Emi1 ternary complex at 3.6 angstrom resolution. EMDB-2925: Cryo-EM structure of the human APC/C-Cdh1-Hsl1-UbcH10-Ub complex. EMDB-2926: |
化合物 | ChemComp-ZN: |
由来 |
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キーワード | CELL CYCLE / UBIQUITINATION / APC/C / APC SUBUNITS / ANAPHASE PROMOTING COMPLEX |