Binding of STIL to PLK4's characteristic Polo-box 3 links PLK4 kinase activation to STIL self-association and is a crucial regulatory step for the localized recruitment of downstream factors in centriole duplication.
Cryo-electron tomography of mammalian and fly centrioles shows that the ninefold symmetry of centrioles is set by species-specific microtubule linkers.
SAS-5 forms oligomers, through a trimeric coiled coil and novel dimeric domain, that are necessary for centriolar localisation of SAS-5 and for centriole duplication.
The previously uncharacterized protein PPP1R35 is a novel centriolar luminal protein critical for centriole elongation by acting in a complex with microcephaly protein RTTN.
Canonical centriole duplication is much less prone to errors than de novo synthesis of centrioles, but neither depends on self-oligomerization of the centriole protein SAS-6.
To control centriole duplication, centriolar satellite proteins assemble a microcephaly-associated protein complex at the centrosome and activate cyclin-dependent kinase 2.
Deletion of delta-tubulin or epsilon-tubulin in human cells results in loss of centriolar triplet microtubules and defects in centriole structure and inheritance.
The structure of the Ana2 Central Coiled-Coil Domain provides insight into how centriolar cartwheel components may be recruited and assembled, and indicates that cartwheel assembly involves more than just SAS-6 oligomerisation.
