Document Type
Article
Language
eng
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
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.
Recommended Citation
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). Biological Sciences Faculty Research and Publications. 305.
https://epublications.marquette.edu/bio_fac/305
Comments
Published version. Molecular Biology of the Cell, Vol. 20, No. 13 (July 2009): 3044-3054. DOI. © 2009 American Society for Cell Biology. Used with permission.