Radial spoke proteins of<i>Chlamydomonas</i>flagella

DOI PDF 16 Citations
  • Pinfen Yang
    Department of Biological Sciences, Marquette University, Milwaukee, WI 53233, USA
  • Dennis R. Diener
    Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520, USA
  • Chun Yang
    Department of Biological Sciences, Marquette University, Milwaukee, WI 53233, USA
  • Takahiro Kohno
    Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, 113-0033, Japan
  • Gregory J. Pazour
    Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA
  • Jennifer M. Dienes
    Department of Biological Sciences, Marquette University, Milwaukee, WI 53233, USA
  • Nathan S. Agrin
    Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA
  • Stephen M. King
    Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030, USA
  • Winfield S. Sale
    Department of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322, USA
  • Ritsu Kamiya
    Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, 113-0033, Japan
  • Joel L. Rosenbaum
    Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520, USA
  • George B. Witman
    Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA

Description

<jats:p>The radial spoke is a ubiquitous component of `9+2' cilia and flagella, and plays an essential role in the control of dynein arm activity by relaying signals from the central pair of microtubules to the arms. The Chlamydomonas reinhardtii radial spoke contains at least 23 proteins, only 8 of which have been characterized at the molecular level. Here, we use mass spectrometry to identify 10 additional radial spoke proteins. Many of the newly identified proteins in the spoke stalk are predicted to contain domains associated with signal transduction, including Ca2+-, AKAP- and nucleotide-binding domains. This suggests that the spoke stalk is both a scaffold for signaling molecules and itself a transducer of signals. Moreover, in addition to the recently described HSP40 family member, a second spoke stalk protein is predicted to be a molecular chaperone, implying that there is a sophisticated mechanism for the assembly of this large complex. Among the 18 spoke proteins identified to date, at least 12 have apparent homologs in humans, indicating that the radial spoke has been conserved throughout evolution. The human genes encoding these proteins are candidates for causing primary ciliary dyskinesia, a severe inherited disease involving missing or defective axonemal structures, including the radial spokes.</jats:p>

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