+Search query
-Structure paper
Title | Atomic structure of the APC/C and its mechanism of protein ubiquitination. |
---|---|
Journal, issue, pages | Nature, Vol. 522, Issue 7557, Page 450-454, Year 2015 |
Publish date | Jun 25, 2015 |
Authors | Leifu Chang / Ziguo Zhang / Jing Yang / Stephen H McLaughlin / David Barford / |
PubMed 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 ...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. |
External links | Nature / PubMed:26083744 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.6 - 7.3 Å |
Structure data | 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: |
Chemicals | ChemComp-ZN: |
Source |
|
Keywords | CELL CYCLE / UBIQUITINATION / APC/C / APC SUBUNITS / ANAPHASE PROMOTING COMPLEX |