TY - JOUR
T1 - IC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding
AU - Wirschell, Maureen
AU - Yang, Chun
AU - Yang, Pinfen
AU - Fox, Laura
AU - Yanagisawa, Haru Aki
AU - Kamiya, Ritsu
AU - Witman, George B.
AU - Porter, Mary E.
AU - Sale, Winfield S.
PY - 2009/7/1
Y1 - 2009/7/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=67650453716&partnerID=8YFLogxK
U2 - 10.1091/mbc.E09-04-0276
DO - 10.1091/mbc.E09-04-0276
M3 - Article
C2 - 19420136
AN - SCOPUS:67650453716
SN - 1059-1524
VL - 20
SP - 3044
EP - 3054
JO - Molecular biology of the cell
JF - Molecular biology of the cell
IS - 13
ER -