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Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella
Lv, Bo1,2; Wan, Lei1; Taschner, Michael3,4; Cheng, Xi1,2; Lorentzen, Esben3,4; Huang, Kaiyao1
2017-05-01
Source PublicationJOURNAL OF CELL SCIENCE
ISSN0021-9533
Volume130Issue:9Pages:1662-1674
AbstractCilia 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 an ift46-1 mutant. The C-terminal sequence between residues 246-321, termed BBTS3, was sufficient to target YFP to basal bodies in the ift46-1 strain. 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.
SubtypeArticle
KeywordChlamydomonas Intraflagellar Transport Basal Body Targeting Sequence
DOI10.1242/jcs.200758
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Indexed BySCI
Funding OrganizationNational Natural Science Foundation of China(31371354) ; National Natural Science Foundation of China(31371354) ; Novo Nordisk Foundation(NNF15OC0014164) ; Novo Nordisk Foundation(NNF15OC0014164) ; National Natural Science Foundation of China(31371354) ; National Natural Science Foundation of China(31371354) ; Novo Nordisk Foundation(NNF15OC0014164) ; Novo Nordisk Foundation(NNF15OC0014164)
Language英语
WOS Research AreaCell Biology
WOS SubjectCell Biology
WOS KeywordCILIARY VESICLE DOCKING ; CHLAMYDOMONAS-REINHARDTII ; PRIMARY CILIUM ; COMPLEX-B ; CELLS ANTENNA ; KINESIN-II ; LOCALIZATION ; DYNEIN ; CORE ; CILIOPATHIES
WOS IDWOS:000402549400015
Funding OrganizationNational Natural Science Foundation of China(31371354) ; National Natural Science Foundation of China(31371354) ; Novo Nordisk Foundation(NNF15OC0014164) ; Novo Nordisk Foundation(NNF15OC0014164) ; National Natural Science Foundation of China(31371354) ; National Natural Science Foundation of China(31371354) ; Novo Nordisk Foundation(NNF15OC0014164) ; Novo Nordisk Foundation(NNF15OC0014164)
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Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/32119
Collection藻类生物学及应用研究中心
Affiliation1.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Hunan, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100039, Peoples R China
3.Max Planck Inst Biochem, Dept Struct Cell Biol, D-82152 Martinsried, Germany
4.Aarhus Univ, Dept Mol Biol & Genet, Gustav Wieds Vej 10c, DK-8000 Aarhus C, Denmark
Recommended Citation
GB/T 7714
Lv, Bo,Wan, Lei,Taschner, Michael,et al. Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella[J]. JOURNAL OF CELL SCIENCE,2017,130(9):1662-1674.
APA Lv, Bo,Wan, Lei,Taschner, Michael,Cheng, Xi,Lorentzen, Esben,&Huang, Kaiyao.(2017).Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella.JOURNAL OF CELL SCIENCE,130(9),1662-1674.
MLA Lv, Bo,et al."Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella".JOURNAL OF CELL SCIENCE 130.9(2017):1662-1674.
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