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Published 5 July 2005. doi:10.1083/jcb.200504008
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 1, 103-113
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Article

 Proteomic analysis of a eukaryotic cilium

Gregory J. Pazour1, Nathan Agrin2, John Leszyk3, and George B. Witman2

1 Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605
2 Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655
3 Proteomic Mass Spectrometry Laboratory, University of Massachusetts Medical School, Shrewsbury, MA 01545

Correspondence to G.B. Witman: george.witman{at}umassmed.edu

Cilia and flagella are widespread cell organelles that have been highly conserved throughout evolution and play important roles in motility, sensory perception, and the life cycles of eukaryotes ranging from protists to humans. Despite the ubiquity and importance of these organelles, their composition is not well known. Here we use mass spectrometry to identify proteins in purified flagella from the green alga Chlamydomonas reinhardtii. 360 proteins were identified with high confidence, and 292 more with moderate confidence. 97 out of 101 previously known flagellar proteins were found, indicating that this is a very complete dataset. The flagellar proteome is rich in motor and signal transduction components, and contains numerous proteins with homologues associated with diseases such as cystic kidney disease, male sterility, and hydrocephalus in humans and model vertebrates. The flagellum also contains many proteins that are conserved in humans but have not been previously characterized in any organism. The results indicate that flagella are far more complex than previously estimated.

G.J. Pazour and N. Agrin contributed equally to this work.

Abbreviations used: FAP, flagellar associated protein; IFT, intraflagellar transport; InsP3, inositol 1,4,5-trisphosphate; MS, mass spectrometry; PKD, polycystic kidney disease; PMCA, plasma membrane Ca2+ ATPase.


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