Leidel, S.Delattre, M.Cerutti, L.Baumer, K.Gönczy, P.2006-08-242006-08-242006-08-24200510.1038/ncb1220https://infoscience.epfl.ch/handle/20.500.14299/23379415665853The mechanisms that ensure centrosome duplication are poorly understood. In Caenorhabditis elegans, ZYG-1, SAS-4, SAS-5 and SPD-2 are required for centriole formation. However, it is unclear whether these proteins have functional homologues in other organisms. Here, we identify SAS-6 as a component that is required for daughter centriole formation in C. elegans. SAS-6 is a coiled-coil protein that is recruited to centrioles at the onset of the centrosome duplication cycle. Our analysis indicates that SAS-6 and SAS-5 associate and that this interaction, as well as ZYG-1 function, is required for SAS-6 centriolar recruitment. SAS-6 is the founding member of an evolutionarily conserved protein family that contains the novel PISA motif. We investigated the function of the human homologue of SAS-6. GFP-HsSAS-6 localizes to centrosomes and its overexpression results in excess foci-bearing centriolar markers. Furthermore, siRNA-mediated inactivation of HsSAS-6 in U2OS cells abrogates centrosome overduplication following aphidicolin treatment and interferes with the normal centrosome duplication cycle. Therefore, HsSAS-6 is also required for centrosome duplication, indicating that the function of SAS-6-related proteins has been widely conserved during evolution.Amino Acid SequenceAnimalsAphidicolin/pharmacologyCaenorhabditis elegans/*metabolismCaenorhabditis elegans Proteins/*physiologyCell Cycle Proteins/*physiologyCentrioles/*physiologyCentrosome/*physiologyConserved SequenceHumansMembrane Proteins/metabolismMolecular Sequence DataSequence Alignmenttext::journal::journal article::research article