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Publication : Cep120 is asymmetrically localized to the daughter centriole and is essential for centriole assembly.

First Author  Mahjoub MR Year  2010
Journal  J Cell Biol Volume  191
Issue  2 Pages  331-46
PubMed ID  20956381 Mgi Jnum  J:165482
Mgi Id  MGI:4837558 Doi  10.1083/jcb.201003009
Citation  Mahjoub MR, et al. (2010) Cep120 is asymmetrically localized to the daughter centriole and is essential for centriole assembly. J Cell Biol 191(2):331-46
abstractText  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.
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