title: Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella.
abstract: Cilia are microtubule-based organelles and perform motile, sensing and signaling functions. The assembly and maintenance of cilia depend on intraflagellar transport (IFT). Besides ciliary localization, most IFT proteins accumulate at basal bodies. However, little is known about the molecular mechanism of basal body targeting of IFT proteins. We first identified the possible basal body-targeting sequence in IFT46 by expressing IFT46 truncation constructs in anift46-1mutant. The C-terminal sequence between residues 246-321, termed BBTS3, was sufficient to target YFP to basal bodies in theift46-1strain. Interestingly, BBTS3 is also responsible for the ciliary targeting of IFT46. BBTS3::YFP moves bidirectionally in flagella and interacts with other IFT complex B (IFT-B) proteins. Using IFT and motor mutants, we show that the basal body localization of IFT46 depends on IFT52, but not on IFT81, IFT88, IFT122, FLA10 or DHC1b. IFT52 interacts with IFT46 through residues L285 and L286 of IFT46 and recruits it to basal bodies. Ectopic expression of the C-terminal domain of IFT52 in the nucleus resulted in accumulation of IFT46 in nuclei. These data suggest that IFT52 and IFT46 can preassemble as a complex in the cytoplasm, which is then targeted to basal bodies.
authors.affiliation: Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, Hubei 430072, China.|University of Chinese Academy of Sciences, Beijing 100039, China.
authors.forename: Bo
authors.identifier: 0000-0002-3448-8986
authors.initials: B
authors.lastname: Lv
authors.affiliation: Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, Hubei 430072, China.
authors.forename: Lei
authors.identifier: 0000-0003-2064-9643
authors.initials: L
authors.lastname: Wan
authors.affiliation: Department of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Martinsried D-82152, Germany.
authors.forename: Michael
authors.identifier: 0000-0002-3789-5077
authors.initials: M
authors.lastname: Taschner
authors.affiliation: Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, Hubei 430072, China.|University of Chinese Academy of Sciences, Beijing 100039, China.
authors.forename: Xi
authors.identifier: 0000-0003-2117-4707
authors.initials: X
authors.lastname: Cheng
authors.affiliation: Department of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Martinsried D-82152, Germany.
authors.forename: Esben
authors.identifier: 0000-0001-6493-7220
authors.initials: E
authors.lastname: Lorentzen
authors.affiliation: Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, Hubei 430072, China huangky@ihb.ac.cn.
authors.forename: Kaiyao
authors.identifier: 0000-0001-8669-1065
authors.initials: K
authors.lastname: Huang
mesh_terms: D054468:Axoneme / Q000378:metabolism; D064652:Basal Bodies / Q000378:metabolism*; D002465:Cell Movement; D002467:Cell Nucleus / Q000378:metabolism; D016825:Chlamydomonas reinhardtii / Q000166:cytology / Q000378:metabolism*; D002923:Cilia / Q000378:metabolism; D005407:Flagella / Q000378:metabolism*; D008954:Models, Biological; D019913:Nuclear Localization Signals; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000378:metabolism
chemical_list: D019913:Nuclear Localization Signals; D011993:Recombinant Fusion Proteins
keywords: Basal body; Chlamydomonas; Intraflagellar transport; Targeting sequence