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dc.contributor.authorBrown, Jason M.
dc.contributor.authorCochran, Deborah A.
dc.contributor.authorCraige, Branch
dc.contributor.authorKubo, Tomohiro
dc.contributor.authorWitman, George B.
dc.date2022-08-11T08:08:03.000
dc.date.accessioned2022-08-23T15:40:48Z
dc.date.available2022-08-23T15:40:48Z
dc.date.issued2015-06-15
dc.date.submitted2015-10-13
dc.identifier.citationCurr Biol. 2015 Jun 15;25(12):1583-93. doi: 10.1016/j.cub.2015.04.060. <a href="http://dx.doi.org/10.1016/j.cub.2015.04.060">Link to article on publisher's site</a>.
dc.identifier.issn0960-9822 (Linking)
dc.identifier.doi10.1016/j.cub.2015.04.060
dc.identifier.pmid26051893
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26484
dc.description.abstractIntraflagellar transport (IFT) moves IFT trains carrying cargoes from the cell body into the flagellum and from the flagellum back to the cell body. IFT trains are composed of complexes IFT-A and IFT-B and cargo adaptors such as the BBSome. The IFT-B core proteins IFT74 and IFT81 interact directly through central and C-terminal coiled-coil domains, and recently it was shown that the N termini of these proteins form a tubulin-binding module important for ciliogenesis. To investigate the function of IFT74 and its domains in vivo, we have utilized Chlamydomonas reinhardtii ift74 mutants. In a null mutant, lack of IFT74 destabilized IFT-B, leading to flagella assembly failure. In this null background, expression of IFT74 lacking 130 amino acids (aa) of the charged N terminus stabilized IFT-B and promoted slow assembly of nearly full-length flagella. A further truncation (lacking aa 1-196, including part of coiled-coil 1) also stabilized IFT-B, but failure in IFT-A/IFT-B interaction within the pool at the base of the flagellum prevented entry of IFT-A into the flagellum and led to severely decreased IFT injection frequency and flagellar-assembly defects. Decreased IFT-A in these short flagella resulted in aggregates of stalled IFT-B in the flagella. We conclude that IFT74 is required to stabilize IFT-B; aa 197-641 are sufficient for this function in vivo. The N terminus of IFT74 may be involved in, but is not required for, tubulin entry into flagella. It is required for association of IFT-A and IFT-B at the base of the flagellum and flagellar import of IFT-A.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=26051893&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.cub.2015.04.060
dc.subjectCell Biology
dc.subjectCellular and Molecular Physiology
dc.titleAssembly of IFT trains at the ciliary base depends on IFT74
dc.typeJournal Article
dc.source.journaltitleCurrent biology : CB
dc.source.volume25
dc.source.issue12
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cellbiology_pp/169
dc.identifier.contextkey7709836
html.description.abstract<p>Intraflagellar transport (IFT) moves IFT trains carrying cargoes from the cell body into the flagellum and from the flagellum back to the cell body. IFT trains are composed of complexes IFT-A and IFT-B and cargo adaptors such as the BBSome. The IFT-B core proteins IFT74 and IFT81 interact directly through central and C-terminal coiled-coil domains, and recently it was shown that the N termini of these proteins form a tubulin-binding module important for ciliogenesis. To investigate the function of IFT74 and its domains in vivo, we have utilized Chlamydomonas reinhardtii ift74 mutants. In a null mutant, lack of IFT74 destabilized IFT-B, leading to flagella assembly failure. In this null background, expression of IFT74 lacking 130 amino acids (aa) of the charged N terminus stabilized IFT-B and promoted slow assembly of nearly full-length flagella. A further truncation (lacking aa 1-196, including part of coiled-coil 1) also stabilized IFT-B, but failure in IFT-A/IFT-B interaction within the pool at the base of the flagellum prevented entry of IFT-A into the flagellum and led to severely decreased IFT injection frequency and flagellar-assembly defects. Decreased IFT-A in these short flagella resulted in aggregates of stalled IFT-B in the flagella. We conclude that IFT74 is required to stabilize IFT-B; aa 197-641 are sufficient for this function in vivo. The N terminus of IFT74 may be involved in, but is not required for, tubulin entry into flagella. It is required for association of IFT-A and IFT-B at the base of the flagellum and flagellar import of IFT-A.</p>
dc.identifier.submissionpathcellbiology_pp/169
dc.contributor.departmentDepartment of Cell and Developmental Biology
dc.source.pages1583-93


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