In silico spatial simulations reveal that MCC formation and excess BubR1 are required for tight inhibition of the anaphase-promoting complex

2015 ◽  
Vol 11 (11) ◽  
pp. 2867-2877 ◽  
Author(s):  
Bashar Ibrahim

In response to the activation of the mitotic spindle assembly checkpoint (SAC), distinct inhibitory pathways control the activity of the anaphase-promoting complex (APC/C).

PLoS ONE ◽  
2008 ◽  
Vol 3 (2) ◽  
pp. e1555 ◽  
Author(s):  
Bashar Ibrahim ◽  
Stephan Diekmann ◽  
Eberhard Schmitt ◽  
Peter Dittrich

2021 ◽  
Author(s):  
Thomas Tischer ◽  
Jing Yang ◽  
David Barford

The control of protein abundance is a fundamental regulatory mechanism during mitosis. The anaphase promoting complex/cyclosome (APC/C) is the main protein ubiquitin ligase responsible for the temporal regulation of mitotic progression. It has been proposed that the APC/C might fulfil other functions including assembly of the mitotic spindle. Here, we show that the APC/C localizes to centrosomes, the organizers of the eukaryotic microtubule cytoskeleton, specifically during mitosis. Recruitment of the APC/C to spindle poles requires the centrosomal protein Cep152, and we identified Cep152 as both an APC/C interaction partner and as an APC/C substrate. Previous studies showed that Cep152 forms a complex with Cep57 and Cep63. The APC/C-mediated ubiquitination of Cep152 at the centrosome releases Cep57 from this inhibitory complex and enables its interaction with pericentrin, a critical step in promoting microtubule nucleation. Thus, our study extends the function of the APC/C from being a regulator of mitosis to also acting as a positive governor of spindle assembly. The APC/C thereby integrates control of these two important processes in a temporal manner.


2015 ◽  
Vol 10 (7) ◽  
pp. 1661-1666 ◽  
Author(s):  
Johanna Kastl ◽  
Joachim Braun ◽  
Andreas Prestel ◽  
Heiko M. Möller ◽  
Thomas Huhn ◽  
...  

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