Together, the IFT81 and IFT74 N-termini form the main module for intraflagellar transport of tubulin
Bellve, Karl D.
Craft, Julie M.
Fogarty, Kevin E.
Witman, George B.
Document TypeJournal Article
MetadataShow full item record
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.
J Cell Sci. 2016 May 15;129(10):2106-19. doi: 10.1242/jcs.187120. Epub 2016 Apr 11. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/26492
Related ResourcesLink to Article in PubMed
Publisher PDF posted after 12 months as allowed by the publisher's author rights policy at http://jcs.biologists.org/content/rights-permissions.