IC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding
| dc.contributor.author | Wirschell, Maureen | |
| dc.contributor.author | Yang, Chun | |
| dc.contributor.author | Yang, Pinfen | |
| dc.contributor.author | Fox, Laura | |
| dc.contributor.author | Yanagisawa, Haru-aki | |
| dc.contributor.author | Kamiya, Ritsu | |
| dc.contributor.author | Witman, George B. | |
| dc.contributor.author | Porter, Mary E. | |
| dc.contributor.author | Sale, Winfield S. | |
| dc.date | 2022-08-11T08:11:05.000 | |
| dc.date.accessioned | 2022-08-23T17:33:04Z | |
| dc.date.available | 2022-08-23T17:33:04Z | |
| dc.date.issued | 2009-07-08 | |
| dc.date.submitted | 2011-01-21 | |
| dc.identifier.citation | Mol Biol Cell. 2009 Jul;20(13):3044-54. Epub 2009 May 6. <a href="http://dx.doi.org/10.1091/mbc.E09-04-0276">Link to article on publisher's site</a> | |
| dc.identifier.issn | 1059-1524 (Linking) | |
| dc.identifier.doi | 10.1091/mbc.E09-04-0276 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.14038/51089 | |
| dc.description.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 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. | |
| dc.language.iso | en_US | |
| dc.relation | <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=19420136&dopt=Abstract">Link to Article in PubMed</a> | |
| dc.subject | Algal Proteins | |
| dc.subject | Amino Acid Sequence | |
| dc.subject | Animals | |
| dc.subject | Axoneme | |
| dc.subject | Base Sequence | |
| dc.subject | Blotting, Western | |
| dc.subject | Chlamydomonas reinhardtii | |
| dc.subject | Cloning, Molecular | |
| dc.subject | Dyneins | |
| dc.subject | Immunoprecipitation | |
| dc.subject | Microtubules | |
| dc.subject | Molecular Sequence Data | |
| dc.subject | Mutation | |
| dc.subject | Protein Binding | |
| dc.subject | Protein Subunits | |
| dc.subject | Sequence Analysis, DNA | |
| dc.subject | Sequence Homology, Amino Acid | |
| dc.subject | Tubulin | |
| dc.subject | Cell Biology | |
| dc.title | IC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding | |
| dc.type | Journal Article | |
| dc.source.journaltitle | Molecular biology of the cell | |
| dc.source.volume | 20 | |
| dc.source.issue | 13 | |
| dc.identifier.legacyfulltext | https://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1003&context=witman&unstamped=1 | |
| dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/witman/4 | |
| dc.identifier.contextkey | 1739062 | |
| refterms.dateFOA | 2022-08-23T17:33:04Z | |
| html.description.abstract | <p>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.</p> | |
| dc.identifier.submissionpath | witman/4 | |
| dc.contributor.department | Department of Cell Biology | |
| dc.source.pages | 3044-54 |
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