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Vol. 17, Issue 9, 3781-3792, September 2006
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*Program in Molecular Medicine and Biomedical Imaging Group, Department of Physiology, University of Massachusetts Medical School, Worcester, MA 01605
Submitted February 14, 2006;
Revised May 9, 2006;
Accepted June 5, 2006
Monitoring Editor: Ben Margolis
Eukaryotic cilia are assembled via intraflagellar transport (IFT) in which large protein particles are motored along ciliary microtubules. The IFT particles are composed of at least 17 polypeptides that are thought to contain binding sites for various cargos that need to be transported from their site of synthesis in the cell body to the site of assembly in the cilium. We show here that the IFT20 subunit of the particle is localized to the Golgi complex in addition to the basal body and cilia where all previous IFT particle proteins had been found. In living cells, fluorescently tagged IFT20 is highly dynamic and moves between the Golgi complex and the cilium as well as along ciliary microtubules. Strong knock down of IFT20 in mammalian cells blocks ciliary assembly but does not affect Golgi structure. Moderate knockdown does not block cilia assembly but reduces the amount of polycystin-2 that is localized to the cilia. This work suggests that IFT20 functions in the delivery of ciliary membrane proteins from the Golgi complex to the cilium.
The online version of this contains supplemental material at MBC Online (http://www.molbiolcell.org). This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-02-0133) on June 14, 2006.
Address correspondence to: Gregory J. Pazour (gregory.pazour{at}umassmed.edu)
Abbreviations used: HPA, Helix pomatia agglutinin; IFT, intraflagellar transport; RPE, retinal pigmented epithelium.
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