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J. Biol. Chem., Vol. 280, Issue 30, 27688-27696, July 29, 2005

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Characterization of the Intraflagellar Transport Complex B Core

DIRECT INTERACTION OF THE IFT81 AND IFT74/72 SUBUNITS^*

Ben F. Lucker, Robert H. Behal, Hongmin Qin, Laura C. Siron, W. David Taggart, Joel L. Rosenbaum, and Douglas G. Cole¶

From the Department of Microbiology, Molecular Biology, and Biochemistry and the Center for Reproductive Biology, LSS142, University of Idaho, Moscow, Idaho 83844 and the Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06520

Required for the assembly and maintenance of eukaryotic cilia and flagella, intraflagellar transport (IFT) consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. Anterograde movement of particles away from the cell body is mediated by kinesin-2, whereas retrograde movement away from the flagellar tip is powered by cytoplasmic dynein 1b/2. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits, respectively. In this study, we have used increased ionic strength to remove four peripheral subunits from the IFT complex B of Chlamydomonas reinhardtii, revealing a 500-kDa core that contains IFT88, IFT81, IFT74/72, IFT52, IFT46, and IFT27. This result demonstrates that the complex B subunits, IFT172, IFT80, IFT57, and IFT20 are not required for the core subunits to stay associated. Chemical cross-linking of the complex B core resulted in multiple IFT81-74/72 products. Yeast-based two-hybrid and three-hybrid analyses were then used to show that IFT81 and IFT74/72 directly interact to form a higher order oligomer consistent with a tetrameric complex. Similar analysis of the vertebrate IFT81 and IFT74/72 homologues revealed that this interaction has been evolutionarily conserved. We hypothesize that these proteins form a tetrameric complex, (IFT81)₂(IFT74/72)₂, which serves as a scaffold for the formation of the intact IFT complex B.

Received for publication, May 9, 2005 , and in revised form, June 10, 2005.

^* This work was supported by National Institutes of Health Grants GM14642 (to J. L. R.) and GM61920 and P20RR16454 (to D. G. C.) from the National Center for Research Resources (Biomedical Research Infrastructure Network). 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

^¶ To whom correspondence should be addressed: Dept. of Microbiology, Molecular Biology, and Biochemistry, Life Science South 142, University of Idaho, Moscow, ID 83844-3052. Tel.: 208-885-4071; Fax: 208-885-6518; E-mail: dcole{at}uidaho.edu.

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