IC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding
Authors
Wirschell, MaureenYang, Chun
Yang, Pinfen
Fox, Laura
Yanagisawa, Haru-aki
Kamiya, Ritsu
Witman, George B.
Porter, Mary E.
Sale, Winfield S.
UMass Chan Affiliations
Department of Cell BiologyDocument Type
Journal ArticlePublication Date
2009-07-08Keywords
Algal ProteinsAmino 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
Cell Biology
Metadata
Show full item recordAbstract
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.Source
Mol Biol Cell. 2009 Jul;20(13):3044-54. Epub 2009 May 6. Link to article on publisher's siteDOI
10.1091/mbc.E09-04-0276Permanent Link to this Item
http://hdl.handle.net/20.500.14038/51089Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1091/mbc.E09-04-0276
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