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Steib, E.

Publications and source records attributed to Steib, E..

2 recordsLinked to original sources

CCDC15 localizes to the centriole inner scaffold and regulates centriole integrity and ciliogenesis

Centrioles are evolutionarily conserved microtubule-based organelles critical to form centrosomes and cilia, which act as microtubule-organizing, signaling and motility centers. Biogenesis and maintenance of centrioles with proper number, size and architecture are crucial for their functions during development and physiology. Consequently, their deregulation causes developmental disorders and cancer. Although centriole number control has been extensively studied, less is known about how centrioles are maintained as stable structures with conserved size and architecture over successive cell divisions and upon ciliary and flagellar motility. Here, we addressed this question by identifying and characterizing new components of the centriole inner scaffold, a recently discovered centriolar sub-compartment critical for centriole size control and integrity. To this end, we generated proximity interactomes of Centrin-2 and POC5 and used them to define CCDC15 as a new centriolar protein that co-localizes and interacts with known inner scaffold proteins. Ultrastructure expansion microscopy analysis of CCDC15-depleted cells revealed its functions in centriole length control and integrity, resulting in defective ciliogenesis and Hedgehog signaling. Loss-of-function experiments also defined CCDC15 as a dual regulator for the recruitment of the inner scaffold protein POC1B and the distal SFI1/Centrin complex to the centrioles. Together, our findings uncovered new players and mechanisms of centriole architectural integrity and thereby, provide insights into diseases linked to centriolar defects.

cell biology↗

The inner scaffold protects from centriole fracture

Centrioles are characterized by a nine-fold arrangement of long-lived microtubule triplets that are held together by an inner protein scaffold. These structurally robust organelles experience strenuous cellular processes such as cell division or ciliary beating while performing their function. However, the molecular mechanisms underlying the stability of microtubule triplets, as well as centriole architectural integrity remain poorly understood. Here, using ultrastructure expansion microscopy (U-ExM) for nanoscale protein mapping, we reveal that POC16 and its human homolog WDR90 are components of the centriolar microtubule wall along the central core region of the centriole. We further found that WDR90 is an evolutionary microtubule associated protein with a predicted structurally homology with the ciliary inner junction protein FAP20. Finally, we demonstrate that WDR90 depletion impairs the localization of inner scaffold components, leading to centriole structural abnormalities in both human and Chlamydomonas cells. Altogether, this work highlights that POC16/WDR90 is a crucial evolutionary conserved molecular player participating in centriole architecture integrity.

cell biology↗