Polo kinase recruitment by the protein Spd-2 to the pericentriolar scaffold is a key element of the positive feedback loop which drives the expansion of the mitotic centrosomes in flies.
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.
Building on previous work (Conduit et al., 2014), and contrary to what was previously thought, it is shown that key centrosomal proteins are not recruited to centrosomes as part of large multi-protein assemblies.
During early cortical development, microRNA-128 regulates the homeostasis of neural stem cells by targeting PCM1, a protein that is critical for cell division.
During centrosome maturation, pericentrin is delivered to the centrosome co-translationally by a microtubule- and dynein-dependent process, as pericentrin mRNA is undergoing active translation near the centrosome.
The microtubule organizing potential of the centrosome is inactivated in a stepwise process through phosphatase activity and mechanical disruption to remove an aging matrix of proteins.
The proteins DSpd-2 and Centrosomin assemble into dynamic scaffolds that build from the inside out around the mother centriole and support centrosome maturation.
Myogenin promotes centrosome attenuation and establishes the nuclear envelope as the dominant microtubule organization center via the scaffold protein AKAP6, which is required for the recruitment of centrosomal proteins.
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.
