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.
Microtubules are nucleated by the centrosome of the primary cilium in the apical end-foot of neuroepithelial cells and inter-dependent microtubule and actin dynamics are required here to orchestrate delamination of newborn neurons.
To control centriole duplication, centriolar satellite proteins assemble a microcephaly-associated protein complex at the centrosome and activate cyclin-dependent kinase 2.
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.
Non-centrosomal microtubules are required for endothelial polarization and sprouting, while centrosomally anchored microtubule arrays are both dispensable and insufficient for these processes.
The proteins DSpd-2 and Centrosomin assemble into dynamic scaffolds that build from the inside out around the mother centriole and support centrosome maturation.