PT  - JOURNAL ARTICLE
AU  - Stenzel, Lisa
AU  - Mehler, Judith
AU  - Schreiner, Alina
AU  - Üstüner, Sim
AU  - Zuccoli, Elisa
AU  - Zanin, Esther
AU  - Mikeladze-Dvali, Tamara
TI  - PCMD-1 bridges the centrioles and the PCM scaffold in <em>C. elegans</em>
AID  - 10.1101/2020.11.09.375865
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.11.09.375865
4099  - http://biorxiv.org/content/early/2020/11/10/2020.11.09.375865.short
4100  - http://biorxiv.org/content/early/2020/11/10/2020.11.09.375865.full
AB  - Correct cell division relies on the formation of a bipolar spindle. In animal cells, microtubule nucleation at the spindle poles is facilitated by the pericentriolar material (PCM), which assembles around a pair of centrioles. Although centrioles are essential for PCM assembly, proteins that anchor the PCM to the centrioles are less known. Here we investigate the molecular function of PCMD-1 in bridging the PCM and the centrioles in Caenorhabditis elegans.We demonstrate that centrosomal recruitment of PCMD-1 is dependent on the outer centriolar protein SAS-7. While the most C-terminal part of PCMD-1 is sufficient to target it to the centrosome, the coiled-coil domain promotes its accumulation by facilitating self-interaction. We reveal that PCMD-1 is bridging the centrioles and PCM scaffold through protein-protein interactions with the PCM scaffold protein SPD-5, the mitotic kinase PLK-1 and the centriolar protein SAS-4. Using an ectopic translocation assay, we show that PCMD-1 is able to selectively recruit downstream PCM scaffold components to an ectopic location in the cell, indicating that PCMD-1 is sufficient to anchor the PCM scaffold proteins to the centrioles. Our work suggests that PCMD-1 is an essential functional bridge between the centrioles and the PCM.