Department of Cell Biology
Algal Proteins; Amino Acid Sequence; Animals; Axoneme; Base Sequence; Blotting, Western; Chlamydomonas reinhardtii; Cloning, Molecular; Dyneins; Immunoprecipitation; Microtubules; Molecular Sequence Data; Mutation; Protein Binding; Protein Subunits; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Tubulin
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 alpha- and beta-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.
DOI of Published Version
Mol Biol Cell. 2009 Jul;20(13):3044-54. Epub 2009 May 6. Link to article on publisher's site
Molecular biology of the cell
Wirschell, Maureen; Yang, Chun; Yang, Pinfen; Fox, Laura; Yanagisawa, Haru-aki; Kamiya, Ritsu; Witman, George B.; Porter, Mary E.; and Sale, Winfield S., "IC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding" (2009). Witman Lab Publications. 4.