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CEP192 interacts physically and functionally with the K63-deubiquitinase CYLD to promote mitotic spindle assembly
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Pages 3555 - 3558
http://dx.doi.org/10.4161/cc.21574
Keywords: CEP192, CYLD, K63, centrosome, microtubules, mitosis, proteomics, spindle, ubiquitination
Authors: Maria Ana Gomez-Ferreria, Mikhail Bashkurov, Michael Mullin, Anne-Claude Gingras and Laurence Pelletier
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Abstract:
CEP192 is a centrosome protein that plays a critical role in centrosome biogenesis and function in mammals, Drosophila and C. elegans.1-6 Moreover, CEP192-depleted cells arrest in mitosis with disorganized microtubules, suggesting that CEP192’s function in spindle assembly goes beyond its role in centrosome activity and pointing to a potentially more direct role in the regulation of the mitotic microtubule landscape.7 To better understand CEP192 function in mitosis, we used mass spectrometry to identify CEP192-interacting proteins. We previously reported that CEP192 interacts with NEDD1, a protein that associates with the γ-tubulin ring complex (γ-TuRC) and regulates its phosphorylation status during mitosis.8 Additionally, within the array of proteins that interact with CEP192, we identified the microtubule binding K63-deubiquitinase CYLD. Further analyses show that co-depletion of CYLD alleviates the bipolar spindle assembly defects observed in CEP192-depleted cells. This functional relationship exposes an intriguing role for CYLD in spindle formation and raises the tantalizing possibility that CEP192 promotes robust mitotic spindle assembly by regulating K63-polyubiquitin-mediated signaling through CYLD.
Received: July 11, 2012; Accepted: July 21, 2012; Published Online: August 16, 2012
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