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Targeting of Fzr/Cdh1 for timely activation of the APC/C at the centrosome during mitotic exit
Targeting of Fzr/Cdh1 for timely activation of the APC/C at the centrosome during mitotic exit
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Targeting of Fzr/Cdh1 for timely activation of the APC/C at the centrosome during mitotic exit
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Targeting of Fzr/Cdh1 for timely activation of the APC/C at the centrosome during mitotic exit
Targeting of Fzr/Cdh1 for timely activation of the APC/C at the centrosome during mitotic exit

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Targeting of Fzr/Cdh1 for timely activation of the APC/C at the centrosome during mitotic exit
Targeting of Fzr/Cdh1 for timely activation of the APC/C at the centrosome during mitotic exit
Journal Article

Targeting of Fzr/Cdh1 for timely activation of the APC/C at the centrosome during mitotic exit

2016
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Overview
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/C Fzr 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. The activity of the anaphase-promoting complex/cyclosome (APC/C) needs to be regulated in time and space to perform different functions. Here the authors show that Spd2 localizes the APC/C activator Fzr at the centrosomes to promote optimal APC/C activity towards its centrosomal substrate Aurora A.