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J. Biol. Chem., Vol. 278, Issue 36, 34211-34218, September 5, 2003

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IFT20 Links Kinesin II with a Mammalian Intraflagellar Transport Complex That Is Conserved in Motile Flagella and Sensory Cilia^*

Sheila A. Baker , Katie Freeman , Katherine Luby-Phelps , Gregory J. Pazour  and Joseph C. Besharse  ¶

From the Department of Cell Biology, Neurobiology, and Anatomy, Medical College of Wisconsin, Milwaukee, Wisconsin 53226 and the Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605

Intraflagellar transport (IFT) is an evolutionarily conserved mechanism thought to be required for the assembly and maintenance of all eukaryotic cilia and flagella. Although IFT proteins are present in cells with sensory cilia, the organization of IFT protein complexes in those cells has not been analyzed. To determine whether the IFT complex is conserved in the sensory cilia of photo-receptors, we investigated protein interactions among four mammalian IFT proteins: IFT88/Polaris, IFT57/Hippi, IFT52/NGD5, and IFT20. We demonstrate that IFT proteins extracted from bovine photoreceptor outer segments, a modified sensory cilium, co-fractionate at 17 S, similar to IFT proteins extracted from mouse testis. Using antibodies to IFT88 and IFT57, we demonstrate that all four IFT proteins co-immunoprecipitate from lysates of mouse testis, kidney, and retina. We also extended our analysis to interactions outside of the IFT complex and demonstrate an ATP-regulated co-immunoprecipitation of heterotrimeric kinesin II with the IFT complex. The internal architecture of the IFT complex was investigated using the yeast two-hybrid system. IFT20 exhibited a strong interaction with IFT57/Hippi and the kinesin II subunit, KIF3B. Our data indicate that all four mammalian IFT proteins are part of a highly conserved complex in multiple ciliated cell types. Furthermore, IFT20 appears to bridge kinesin II with the IFT complex.

Received for publication, January 7, 2003 , and in revised form, June 17, 2003.

Note Added in Proof—Additional recent studies on Chlamydomonas reporting co-immunoprecipitation of kinesin II with the IFT complex (Qin, H., Diener, D., Geimer, S., Cole, D., and Rosenbaum, J. (2002) Mol. Biol. Cell 13, 473 (abstract)) and defining additional protein interactions within the complex (Lucker, B. F., Blackmaar, P., Qin, H., Rosenbaum, J. L., and Cole, D. (2002) Mol. Biol. Cell 13, 190 (abstract); Cole, D. (2003) Traffic 4, 436–442) further emphasize the highly conserved nature of IFT among eukaryotes.

^* This work was supported by National Institutes of Health (NIH) Grant EY03222 (to J. C. B.), National Science Foundation Grant MCB-9604594 (to K. L. P.), and NIH Grant GM60992 (to G. J. P.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Dept. of Cell Biology, Neurobiology, and Anatomy, Medical College of Wisconsin, 8701 Watertown Plank Rd., Milwaukee, WI 53226. Tel.: 414-456-8260; Fax: 414-456-6517; E-mail: jbeshars{at}mcw.edu.

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