The Journal of Cell Biology
Department of Biological Sciences
For all motile eukaryotic cilia and flagella, beating is regulated by changes in intraciliary calcium concentration. Although the mechanism for calcium regulation is not understood, numerous studies have shown that calmodulin (CaM) is a key axonemal calcium sensor. Using anti-CaM antibodies and Chlamydomonas reinhardtii axonemal extracts, we precipitated a complex that includes four polypeptides and that specifically interacts with CaM in high [Ca2+]. One of the complex members, FAP221, is an orthologue of mammalian Pcdp1 (primary ciliary dyskinesia protein 1). Both FAP221 and mammalian Pcdp1 specifically bind CaM in high [Ca2+]. Reduced expression of Pcdp1 complex members in C. reinhardtii results in failure of the C1d central pair projection to assemble and significant impairment of motility including uncoordinated bends, severely reduced beat frequency, and altered waveforms. These combined results reveal that the central pair Pcdp1 (FAP221) complex is essential for control of ciliary motility.
DiPetrillo CG, Smith EF. Pcdp1 is a central apparatus protein that binds Ca(2+)-calmodulin and regulates ciliary motility. J Cell Biol. 2010 May 3;189(3):601-12. doi: 10.1083/jcb.200912009. Epub 2010 Apr 26. PMID: 20421426; PMCID: PMC2867295.
Dartmouth Digital Commons Citation
DiPetrillo, Christen G. and Smith, Elizabeth F., "Pcdp1 is a Central Apparatus Protein that Binds Ca2+-Calmodulin and Regulates Ciliary Motility" (2010). Dartmouth Scholarship. 1492.