Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 19, Issue 11, Pages 1116-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2412
Keywords
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Funding
- Boehringer Ingelheim
- Vienna Science and Technology Fund [WWTF LS09-13]
- Laura Bassi Center for Optimized Structural Studies [FFG 822736]
- Austrian Science Fund (FWF) [SFB F34, W1221, Z196-B20]
- European Community [241548 (MitoSys), 262067 (PRIME-XS)]
- American Lebanese Syrian Associated Charities/St. Jude
- Howard Hughes Medical Institute
- German Research Foundation (DFG) [SFB860]
- Japan Society for the Promotion of Science
- Jane Coffin Childs Memorial Fund for Medical Research
- Austrian Science Fund (FWF) [W1221] Funding Source: Austrian Science Fund (FWF)
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The anaphase-promoting complex/cyclosome (APC/C) bound to CDC20 (APC/C-CDC20) initiates anaphase by ubiquitylating B-type cyclins and securin. During chromosome bi-orientation, CDC20 assembles with MAD2, BUBR1 and BUB3 into a mitotic checkpoint complex (MCC) that inhibits substrate recruitment to the APC/C. APC/C activation depends on MCC disassembly, which was proposed to require CDC20 autoubiquitylation. Here we characterize APC15, a human APC/C subunit related to yeast Mnd2. APC15 is located near APC/C's MCC binding site; it is required for APC/C-bound MCC (APC/C-MCC)-dependent CDC20 autoubiquitylation and degradation and for timely anaphase initiation but is dispensable for substrate ubiquitylation by APC/C-CDC20 and APC/C-CDH1. Our results support the model wherein MCC is continuously assembled and disassembled to enable rapid activation of APC/C-CDC20 and CDC20 autoubiquitylation promotes MCC disassembly. We propose that APC15 and Mnd2 negatively regulate APC/C coactivators and report generation of recombinant human APC/C.
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