Cep120 is asymmetrically localized to the daughter centriole and is essential for centriole assembly.
Centrioles form the core of the centrosome in animal cells and function as basal bodies that nucleate and anchor cilia at the plasma membrane. In this paper, we report that Cep120 (Ccdc100), a protein previously shown to be involved in maintaining the neural progenitor pool in mouse brain, is associated with centriole structure and function. Cep120 is up-regulated sevenfold during differentiation of mouse tracheal epithelial cells (MTECs) and localizes to basal bodies. Cep120 localizes preferentially to the daughter centriole in cycling cells, and this asymmetry between mother and daughter centrioles is relieved coincident with new centriole assembly. Photobleaching recovery analysis identifies two pools of Cep120, differing in their halftime at the centriole. We find that Cep120 is required for centriole duplication in cycling cells, centriole amplification in MTECs, and centriole overduplication in S phase-arrested cells. We propose that Cep120 is required for centriole assembly and that the observed defect in neuronal migration might derive from a defect in this process.
Department of Biology, Stanford University, Stanford, CA 94305, USA.
Moe R
MR
Mahjoub
Zhigang
Z
Xie
Tim
T
Stearns
D000818:Animals; D002453:Cell Cycle; D018797:Cell Cycle Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D002454:Cell Differentiation; D016764:Cell Polarity; D002478:Cells, Cultured; D002502:Centrioles / Q000378:metabolism* / Q000648:ultrastructure; D002923:Cilia; D004847:Epithelial Cells / Q000378:metabolism; D036681:Fluorescence Recovery After Photobleaching; D006801:Humans; D051379:Mice; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D015854:Up-Regulation
D018797:Cell Cycle Proteins; C525527:Cep120 protein, mouse