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

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....

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Bibliographic Details
Published in:Experimental cell research 2008-12, Vol.314 (20), p.3692-3700
Main Authors: Kim, Kyeongmi, Lee, Seongju, Chang, Jaerak, Rhee, Kunsoo
Format: Article
Language:English
Subjects:
Autoantigens - metabolism
C-NAP1
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
Cellular biology
Centrioles - metabolism
Centrosome
Centrosome split
CEP135
HeLa Cells
Humans
Models, Biological
Mutant Proteins - genetics
Mutant Proteins - metabolism
Mutation
Protein Binding
Protein Transport
Proteins
Proteomics
Transfection
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Summary: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.
ISSN:0014-4827
1090-2422
DOI:10.1016/j.yexcr.2008.09.016