During early cortical development, microRNA-128 regulates the homeostasis of neural stem cells by targeting PCM1, a protein that is critical for cell division.

In the absence of centrioles, components of pericentriolar material can self-organize into a single compact microtubule-organizing center through dynein-mediated transport of pericentrin-containing protein complexes if CAMSAP- and Golgi-mediated pathways of microtubule minus-end stabilization and anchoring are disabled.

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.

Ciliogenesis requires a gap junction protein (GJA1) mediated ciliary vesicle deposition and CP110 removal.

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 proteins DSpd-2 and Centrosomin assemble into dynamic scaffolds that build from the inside out around the mother centriole and support centrosome maturation.

Cells have evolved a mechanism that actively regulates centriole maturation during quiescence.

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.

Kazrin, a protein widely expressed in vertebrates whose depletion causes defects in cell adhesion and migration, is recruited to early endosomes and promotes dynein/dynactin-dependent traffic of endocytosed cargo to the recycling endosomes.

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.