PCMD-1 bridges the centrioles and the pericentriolar material scaffold in C. elegans

Development. 2021 Oct 15;148(20):dev198416. doi: 10.1242/dev.198416. Epub 2021 Oct 19.


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.

Keywords: Centrioles; Centrosome; PCM; PCMD-1; PLK-1; SPD-5.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans Proteins / metabolism*
  • Cell Cycle Proteins / metabolism*
  • Cell Line
  • Centrioles / metabolism*
  • Centrosome / metabolism
  • HEK293 Cells
  • Humans
  • Mitosis / physiology
  • Protein Serine-Threonine Kinases / metabolism
  • Spindle Poles / metabolism


  • Caenorhabditis elegans Proteins
  • Cell Cycle Proteins
  • PCMD-1 protein, C elegans
  • SAS-4 protein, C elegans
  • Protein Serine-Threonine Kinases
  • plk-1 protein, C elegans