Show simple item record

dc.contributor.authorKubo, Tomohiro
dc.contributor.authorBrown, Jason
dc.contributor.authorBellve, Karl D.
dc.contributor.authorCraige, Branch
dc.contributor.authorCraft, Julie M.
dc.contributor.authorFogarty, Kevin E.
dc.contributor.authorLechtreck, Karl-Ferdinand
dc.contributor.authorWitman, George B.
dc.date2022-08-11T08:08:03.000
dc.date.accessioned2022-08-23T15:40:51Z
dc.date.available2022-08-23T15:40:51Z
dc.date.issued2016-05-15
dc.date.submitted2016-05-31
dc.identifier.citation<p>J Cell Sci. 2016 May 15;129(10):2106-19. doi: 10.1242/jcs.187120. Epub 2016 Apr 11. <a href="http://dx.doi.org/10.1242/jcs.187120">Link to article on publisher's site</a></p>
dc.identifier.issn0021-9533 (Linking)
dc.identifier.doi10.1242/jcs.187120
dc.identifier.pmid27068536
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26492
dc.description.abstractThe assembly and maintenance of most cilia and flagella rely on intraflagellar transport (IFT). Recent in vitro studies have suggested that, together, the calponin-homology domain within the IFT81 N-terminus and the highly basic N-terminus of IFT74 form a module for IFT of tubulin. By using Chlamydomonas mutants for IFT81 and IFT74, we tested this hypothesis in vivo Modification of the predicted tubulin-binding residues in IFT81 did not significantly affect basic anterograde IFT and length of steady-state flagella but slowed down flagellar regeneration, a phenotype similar to that seen in a strain that lacks the IFT74 N-terminus. In both mutants, the frequency of tubulin transport by IFT was greatly reduced. A double mutant that combined the modifications to IFT81 and IFT74 was able to form only very short flagella. These results indicate that, together, the IFT81 and IFT74 N-termini are crucial for flagellar assembly, and are likely to function as the main module for IFT of tubulin.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=27068536&dopt=Abstract">Link to Article in PubMed</a>
dc.rights<p>Publisher PDF posted after 12 months as allowed by the publisher's author rights policy at http://jcs.biologists.org/content/rights-permissions.</p>
dc.subjectCell Biology
dc.subjectCellular and Molecular Physiology
dc.subjectDevelopmental Biology
dc.titleTogether, the IFT81 and IFT74 N-termini form the main module for intraflagellar transport of tubulin
dc.typeJournal Article
dc.source.journaltitleJournal of cell science
dc.source.volume129
dc.source.issue10
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1175&amp;context=cellbiology_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cellbiology_pp/176
dc.legacy.embargo2017-05-15T00:00:00-07:00
dc.identifier.contextkey8667028
refterms.dateFOA2022-08-23T15:40:51Z
html.description.abstract<p>The assembly and maintenance of most cilia and flagella rely on intraflagellar transport (IFT). Recent in vitro studies have suggested that, together, the calponin-homology domain within the IFT81 N-terminus and the highly basic N-terminus of IFT74 form a module for IFT of tubulin. By using Chlamydomonas mutants for IFT81 and IFT74, we tested this hypothesis in vivo Modification of the predicted tubulin-binding residues in IFT81 did not significantly affect basic anterograde IFT and length of steady-state flagella but slowed down flagellar regeneration, a phenotype similar to that seen in a strain that lacks the IFT74 N-terminus. In both mutants, the frequency of tubulin transport by IFT was greatly reduced. A double mutant that combined the modifications to IFT81 and IFT74 was able to form only very short flagella. These results indicate that, together, the IFT81 and IFT74 N-termini are crucial for flagellar assembly, and are likely to function as the main module for IFT of tubulin.</p>
dc.identifier.submissionpathcellbiology_pp/176
dc.contributor.departmentBiomedical Imaging Group
dc.contributor.departmentDepartment of Cell and Developmental Biology
dc.source.pages2106-19


Files in this item

Thumbnail
Name:
2106.full.pdf
Size:
5.073Mb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record