Abstract
Most mammalian cells have a non-motile primary cilium projecting from their apical surface. The importance of these organelles to mammalian health and development has been highlighted by analysis of the Tg737orpk mouse. This mouse develops cysts in the liver, kidney, and pancreas and exhibits hydrocephalus, polydactyly, retinal degeneration, and male sterility. The defective gene in this mouse encodes the IFT88 subunit of the intraflagellar transport (IFT) particle (Pazour et al., J. Cell Biol. 151:–718). IFT is required for assembly of most types of eukaryotic cilia, and the Tg737 mouse has ciliary assembly defects throughout the body. To further our understanding of cilia, we used mass spectrometry to identify the proteome of this organelle purified from Chlamydomonas; because the cilium has been conserved throughout evolution, the mammalian homologues of most Chlamydomonas flagellar proteins are readily identified. 652 proteins were identified, including 97 out of 101 known Chlamydomonas flagellar proteins, indicating that the proteome is very complete. Included in the data set were orthologues of several cystic kidney disease gene products, including polycystin-2 and fibrocystin. Also included were a large number of previously characterized proteins that had not been known to be components of cilia, and ~100 proteins that are highly conserved in ciliated eukaryotes but not characterized in any organism.
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