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dc.contributor.authorWirschell, Maureen
dc.contributor.authorYang, Chun
dc.contributor.authorYang, Pinfen
dc.contributor.authorFox, Laura
dc.contributor.authorYanagisawa, Haru-aki
dc.contributor.authorKamiya, Ritsu
dc.contributor.authorWitman, George B.
dc.contributor.authorPorter, Mary E.
dc.contributor.authorSale, Winfield S.
dc.date2022-08-11T08:11:05.000
dc.date.accessioned2022-08-23T17:33:04Z
dc.date.available2022-08-23T17:33:04Z
dc.date.issued2009-07-08
dc.date.submitted2011-01-21
dc.identifier.citationMol 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.issn1059-1524 (Linking)
dc.identifier.doi10.1091/mbc.E09-04-0276
dc.identifier.urihttp://hdl.handle.net/20.500.14038/51089
dc.description.abstractOur 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.isoen_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.subjectAlgal Proteins
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectAxoneme
dc.subjectBase Sequence
dc.subjectBlotting, Western
dc.subjectChlamydomonas reinhardtii
dc.subjectCloning, Molecular
dc.subjectDyneins
dc.subjectImmunoprecipitation
dc.subjectMicrotubules
dc.subjectMolecular Sequence Data
dc.subjectMutation
dc.subjectProtein Binding
dc.subjectProtein Subunits
dc.subjectSequence Analysis, DNA
dc.subjectSequence Homology, Amino Acid
dc.subjectTubulin
dc.subjectCell Biology
dc.titleIC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding
dc.typeJournal Article
dc.source.journaltitleMolecular biology of the cell
dc.source.volume20
dc.source.issue13
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1003&amp;context=witman&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/witman/4
dc.identifier.contextkey1739062
refterms.dateFOA2022-08-23T17:33:04Z
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.submissionpathwitman/4
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages3044-54


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