The CSC proteins FAP61 and FAP251 build the basal substructures of radial spoke 3 in cilia

Paulina Urbanska, Kangkang Song, Ewa Joachimiak, Lucja Krzemien-Ojak, Piotr Koprowski, Todd Hennessey, Maria Jerka-Dziadosz, Hanna Fabczak, Jacek Gaertig, Daniela Nicastro, Dorota Wloga

Research output: Contribution to journalArticlepeer-review

42 Scopus citations


Dynein motors and regulatory complexes repeat every 96 nm along the length of motile cilia. Each repeat contains three radial spokes, RS1, RS2, and RS3, which transduct signals between the central microtubules and dynein arms. Each radial spoke has a distinct structure, but little is known about the mechanisms of assembly and function of the individual radial spokes. In Chlamydomonas, calmodulin and spoke-associated complex (CSC) is composed of FAP61, FAP91, and FAP251 and has been linked to the base of RS2 and RS3. We show that in Tetrahymena, loss of either FAP61 or FAP251 reduces cell swimming and affects the ciliary waveform and that RS3 is either missing or incomplete, whereas RS1 and RS2 are unaffected. Specifically, FAP251-null cilia lack an arch-like density at the RS3 base, whereas FAP61-null cilia lack an adjacent portion of the RS3 stem region. This suggests that the CSC proteins are crucial for stable and functional assembly of RS3 and that RS3 and the CSC are important for ciliary motility.

Original languageEnglish (US)
Pages (from-to)1463-1475
Number of pages13
JournalMolecular biology of the cell
Issue number8
StatePublished - Apr 15 2015

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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