Stenzel L, Schreiner A, Zuccoli E, Üstüner S, Mehler J, Zanin E, Mikeladze-Dvali T (2021)
Publication Status: Published
Publication Type: Journal article, Original article
Publication year: 2021
Book Volume: 148
Journal Issue: 20
DOI: 10.1242/dev.198416
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, the 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 the centrosomal recruitment of PCMD-1 is dependent on the outer centriolar protein SAS-7. The most C-terminal part of PCMD-1 is sufficient to target it to the centrosome, and the coiled-coil domain promotes its accumulation by facilitating self-interaction. We reveal that PCMD-1 interacts 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 can selectively recruit downstream PCM scaffold components to an ectopic location in the cell, indicating that PCMD-1 is able to anchor the PCM scaffold proteins at the centrioles. Our work suggests that PCMD-1 is an essential functional bridge between the centrioles and the PCM.
APA:
Stenzel, L., Schreiner, A., Zuccoli, E., Üstüner, S., Mehler, J., Zanin, E., & Mikeladze-Dvali, T. (2021). PCMD-1 bridges the centrioles and the pericentriolar material scaffold in C. elegans. Development, 148(20). https://dx.doi.org/10.1242/dev.198416
MLA:
Stenzel, Lisa, et al. "PCMD-1 bridges the centrioles and the pericentriolar material scaffold in C. elegans." Development 148.20 (2021).
BibTeX: Download