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. 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.
Department of Biological Sciences and Research Center for Functional Cellulomics, Seoul National University, Seoul 151-747, Republic of Korea.
Kyeongmi
K
Kim
Seongju
S
Lee
Jaerak
J
Chang
Kunsoo
K
Rhee
D001324:Autoantigens / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D002455:Cell Division / Q000502:physiology; D002478:Cells, Cultured; D002502:Centrioles / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D008954:Models, Biological; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D021381:Protein Transport; D014162:Transfection
D001324:Autoantigens; C534330:CEP135 protein, human; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; C111329:CEP250 protein, human; D050505:Mutant Proteins