期刊
NATURE COMMUNICATIONS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12607
关键词
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资金
- Cancer Research UK Career Development Fellowship
- BBSRC
- Medical Research Council (MRC) Project Grant
- Japan Society for the Promotion of Science
- European Commission
- Biotechnology and Biological Sciences Research Council [BB/I013938/1] Funding Source: researchfish
- Cancer Research UK [12874] Funding Source: researchfish
- Medical Research Council [MR/M010899/1] Funding Source: researchfish
- BBSRC [BB/I013938/1] Funding Source: UKRI
- MRC [MR/M010899/1] Funding Source: UKRI
A multi-subunit ubiquitin ligase, the anaphase-promoting complex/cyclosome (APC/C), regulates critical cellular processes including the cell cycle. To accomplish its diverse functions, APC/C activity must be precisely regulated in time and space. The interphase APC/C activator Fizzy-related (Fzr or Cdh1) is localized at centrosomes in animal cells. However, neither the mechanism of its localization nor its importance is clear. Here we identify the centrosome component Spd2 as a major partner of Fzr in Drosophila. The localization of Fzr to the centriole during interphase depends on direct interaction with Spd2. By generating Spd2 mutants unable to bind Fzr, we show that centrosomal localization of Fzr is essential for optimal APC/C activation towards its centrosomal substrate Aurora A. Finally, we show that Spd2 is also a novel APC/CFzr substrate. Our study is the first to demonstrate the critical importance of distinct subcellular pools of APC/C activators in the spatiotemporal control of APC/C activity.
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