Together, the IFT81 and IFT74 N-termini form the main module for intraflagellar transport of tubulin
dc.contributor.author | Kubo, Tomohiro | |
dc.contributor.author | Brown, Jason | |
dc.contributor.author | Bellve, Karl D. | |
dc.contributor.author | Craige, Branch | |
dc.contributor.author | Craft, Julie M. | |
dc.contributor.author | Fogarty, Kevin E. | |
dc.contributor.author | Lechtreck, Karl-Ferdinand | |
dc.contributor.author | Witman, George B. | |
dc.date | 2022-08-11T08:08:03.000 | |
dc.date.accessioned | 2022-08-23T15:40:51Z | |
dc.date.available | 2022-08-23T15:40:51Z | |
dc.date.issued | 2016-05-15 | |
dc.date.submitted | 2016-05-31 | |
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.issn | 0021-9533 (Linking) | |
dc.identifier.doi | 10.1242/jcs.187120 | |
dc.identifier.pmid | 27068536 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/26492 | |
dc.description.abstract | 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. | |
dc.language.iso | en_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.subject | Cell Biology | |
dc.subject | Cellular and Molecular Physiology | |
dc.subject | Developmental Biology | |
dc.title | Together, the IFT81 and IFT74 N-termini form the main module for intraflagellar transport of tubulin | |
dc.type | Journal Article | |
dc.source.journaltitle | Journal of cell science | |
dc.source.volume | 129 | |
dc.source.issue | 10 | |
dc.identifier.legacyfulltext | https://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1175&context=cellbiology_pp&unstamped=1 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/cellbiology_pp/176 | |
dc.legacy.embargo | 2017-05-15T00:00:00-07:00 | |
dc.identifier.contextkey | 8667028 | |
refterms.dateFOA | 2022-08-23T15:40:51Z | |
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.submissionpath | cellbiology_pp/176 | |
dc.contributor.department | Biomedical Imaging Group | |
dc.contributor.department | Department of Cell and Developmental Biology | |
dc.source.pages | 2106-19 |
Files in this item
This item appears in the following Collection(s)
-
UMass Chan Faculty and Researcher Publications [16003]
-
Witman Lab [126]