A novel function of CEP135 as a platform protein of C-NAP1 for its centriolar localization

Exp Cell Res. 2008 Dec 10;314(20):3692-700. doi: 10.1016/j.yexcr.2008.09.016. Epub 2008 Oct 1.

Abstract

A proteomic study predicted that about one hundred kinds of proteins constitute a basic structure of the centrosome. Most of the core centrosomal proteins contain extensive coiled-coil domains, suggesting that the protein-protein interaction is a critical force for the core centrosome configuration. In the present study, we investigated a novel interaction between CEP135 and C-NAP1, two core centriolar proteins. Depletion of CEP135 caused a premature centrosome splitting. Reduction of the centrosomal C-NAP1 level was accompanied in a specific manner. Ectopic expression of the CEP135 mutant proteins also caused centrosome splitting in association with the reduction of the centrosomal C-NAP1 levels. Based on these results, we propose that CEP135 acts as a platform protein for C-NAP1 at the centriole.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autoantigens / metabolism*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Carrier Proteins / physiology*
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cell Cycle Proteins / physiology
  • Cell Division / physiology
  • Cells, Cultured
  • Centrioles / metabolism*
  • HeLa Cells
  • Humans
  • Models, Biological
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism
  • Protein Binding
  • Protein Transport
  • Transfection

Substances

  • Autoantigens
  • CEP135 protein, human
  • Carrier Proteins
  • Cell Cycle Proteins
  • CEP250 protein, human
  • Mutant Proteins