Atomic structure of the APC/C and its mechanism of protein ubiquitination

Leifu Chang, Ziguo Zhang, Jing Yang, Stephen H. McLaughlin and David Barford ()
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Leifu Chang: MRC Laboratory of Molecular Biology
Ziguo Zhang: MRC Laboratory of Molecular Biology
Jing Yang: MRC Laboratory of Molecular Biology
Stephen H. McLaughlin: MRC Laboratory of Molecular Biology
David Barford: MRC Laboratory of Molecular Biology

Nature, 2015, vol. 522, issue 7557, 450-454

Abstract: Abstract 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.

Date: 2015
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DOI: 10.1038/nature14471

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