Centriole amplification is controlled by two duplicated genes, Cep63 (centrosomal protein of 63kDa) and Deup1 (Deuterosome assembly protein 1).Cep63 regulates mother-centriole-dependent centriole duplication, whereas Deup1 is involved in large-scale de novo centriole biogenesis. Deup1, previously known as coiled-coil domain-containing protein 67, is a structural component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells. Deup1 binds to Cep152 and then recruits Plk4 to activate centriole biogenesis [].
This entry represents the N-terminal domain of the centrosomal proteins Cep63 and Deup1. Cep63 regulates mother-centriole-dependent centriole duplication, whereas Deup1 governs deuterosome assembly for large-scale de novo centriole biogenesis [].
Centriole amplification is controlled by two duplicated genes, Cep63 and Deup1. Cep63 regulates mother-centriole-dependent centriole duplication, whereas Deup1 governs deuterosome assembly for large-scale de novo centriole biogenesis in vertebrate multiciliate cells [].Cep63 functions to ensure that centriole duplication occurs reliably in dividing cells. It interacts and cooperates with Cep152. Both proteins are dependent on one another for centrosomal localisation []. Cep57-Cep63-Cep152 form a ring-like complex that localises around the proximal end of centrioles []. Cep63 recruits Cdk1, which is essential for mitotic entry, providing a link between the centrosome and the cell-cycle machinery [].
