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Vol. 20, Issue 13, 3044-3054, July 1, 2009
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*Department of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322; Department of Biology, Marquette University, Milwaukee, WI 53201; Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan; Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655; and ||Department of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, MN 55455
Submitted April 8, 2009;
Revised April 23, 2009;
Accepted April 29, 2009
Monitoring Editor: Erika Holzbaur
Our goal is to understand the assembly and regulation of flagellar dyneins, particularly the Chlamydomonas inner arm dynein called I1 dynein. Here, we focus on the uncharacterized I1-dynein IC IC97. The IC97 gene encodes a novel IC without notable structural domains. IC97 shares homology with the murine lung adenoma susceptibility 1 (Las1) protein—a candidate tumor suppressor gene implicated in lung tumorigenesis. Multiple, independent biochemical assays determined that IC97 interacts with both 
- and β-tubulin subunits within the axoneme. I1-dynein assembly mutants suggest that IC97 interacts with both the IC138 and IC140 subunits within the I1-dynein motor complex and that IC97 is part of a regulatory complex that contains IC138. Microtubule sliding assays, using axonemes containing I1 dynein but devoid of IC97, show reduced microtubule sliding velocities that are not rescued by kinase inhibitors, revealing a critical role for IC97 in I1-dynein function and control of dynein-driven motility.
Address correspondence to: Winfield S. Sale (win{at}cellbio.emory.edu)
Abbreviations used: bop, bypass of paralysis; FAP, flagellar associated protein; HC, heavy chain; IC, intermediate chain; LC, light chain; PKI, protein kinase inhibitor.
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