Mar 5, 2014

Negative feedback between the APC/C and Cep152 at the centrosome regulates mitotic spindle assembly

BioRxiv : the Preprint Server for Biology
Anze ZupanicDaryl P Shanley

Abstract

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 regulating mitotic progression in a timely manner. Previous studies proposed that the spatial regulation of protein degradation also plays an important role during mitosis. Here, we show that the APC/C localizes to centrosomes, the organizers of the eukaryotic microtubule cytoskeleton, specifically during mitosis. The APC/C is recruited to spindle poles by the centrosomal protein Cep152. We not only identify Cep152 as a novel APC/C interaction partner, but also as an APC/C substrate. Importantly, the APC/C-dependent degradation of Cep152 creates a negative feedback loop that controls Cep152 removal from spindle poles during mitosis. We show that persistent Cep152 at the centrosome sequesters Cep57 into a complex and away from pericentrin, thereby inhibiting microtubule nucleation. Thus, our study establishes how the APC/C is recruited to the centrosome, and extends its function from being a critical regulator of mitosis to working as a positive governor of spindle assembly.

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Mentioned in this Paper

Study
Post-Transcriptional Regulation
Genome
Genes
Sep15
Regulation of Biological Process
ATF4 gene
Profile (Lab Procedure)
ATF4
Translational Regulation

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