期刊
TRENDS IN CELL BIOLOGY
卷 29, 期 2, 页码 117-134出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2018.09.007
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类别
资金
- NIH [R35GM128855]
- UCRF
- Boehringer Ingelheim
- Austrian Science Fund
- Austrian Research Promotion Agency
- European Community
- Max Planck Society
- ALSAC [NIH R37GM065930, P30CA021765]
The anaphase promoting corn plex/cyclosome (APC/C) E3 ligase controls mitosis and nonmitotic pathways through interactions with proteins that coordinate ubiquitylation. Since the discovery that the catalytic subunits of APC/C are conformationally dynamic cullin and RING proteins, many unexpected and intricate regulatory mechanisms have emerged. Here, we review structural knowledge of this regulation, focusing on: (i) coactivators, E2 ubiquitin (Ub)-conjugating enzymes, and inhibitors engage or influence multiple sites on APC/C including the cullin RING catalytic core; and (ii) the outcomes of these interactions rely on mobility of coactivators and cullin RING domains, which permits distinct conformations specifying different functions. Thus, APC/C is not simply an interaction hub, but is instead a dynamic, multifunctional molecular machine whose structure is remodeled by binding partners to achieve temporal ubiquitylation regulating cell division.
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