CEP192 interacts physically and functionally with the K63-deubiquitinase CYLD to promote mitotic spindle assembly

Cell Cycle. 2012 Oct 1;11(19):3555-8. doi: 10.4161/cc.21574. Epub 2012 Aug 16.


CEP192 is a centrosome protein that plays a critical role in centrosome biogenesis and function in mammals, Drosophila and C. elegans. 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. 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. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromosomal Proteins, Non-Histone / metabolism*
  • Deubiquitinating Enzyme CYLD
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Immunoprecipitation
  • Lysine / metabolism*
  • Mass Spectrometry
  • Protein Binding
  • Spindle Apparatus / metabolism*
  • Tumor Suppressor Proteins / metabolism*


  • Cep192 protein, human
  • Chromosomal Proteins, Non-Histone
  • Tumor Suppressor Proteins
  • CYLD protein, human
  • Deubiquitinating Enzyme CYLD
  • Lysine