Document Type

Article

Language

eng

Format of Original

11 p.

Publication Date

7-2009

Publisher

American Society for Cell Biology

Source Publication

Molecular Biology of the Cell

Source ISSN

1059-1524

Original Item ID

doi: 10.1091/mbc.E09-04-0276; PubMed Central, PMCID: PMC2704156

Abstract

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 α- 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.

Comments

Published version. Molecular Biology of the Cell, Vol. 20, No. 13 (July 2009): 3044-3054. DOI. © American Society for Cell Biology 2009. Used with permission.

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