Structural analyses of the centriole proteins CPAP and STIL identify domains that are critical for centriole formation and provide a structural explanation for a mutation that causes human microcephaly.
A genetic screen and live cell imaging show that a newly identified coiled-coil protein called SAS-7 is the earliest acting factor in centriole assembly yet identified in the roundworm Caenorhabditis elegans.
Newly discovered interaction between fission yeast SPB and animal centriole components reveals that pericentrin not only functions as a microtubule-nucleator, but also promotes centriole assembly in animals.
Alms1a is a centrosomal protein that exhibits asymmetric localization between mother and daughter centrosomes in asymmetrically dividing stem cells in Drosophila testis, controlling centriole duplication.
Building on previous work (Doroquez et al., 2014), it is shown that the centriole core of the basal body degenerates, but the outer wall remodels to template the ciliary axoneme in a subset of C. elegans ciliated sensory neurons.
At optimal concentrations, the ciliary inhibitor Cp110 promotes ciliogenesis by localization to previously uncharacterized sites at the basal body, where it recruits ciliary adhesion complexes that mediate basal body interaction with F-actin networks.