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  Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella

Lv, B., Wan, L., Taschner, M., Cheng, X., Lorentzen, E., & Huang, K. (2017). Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella. Journal of Cell Science, 130(9), 1662-1674. doi:10.1242/jcs.200758.

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 Urheber:
Lv, Bo1, Autor
Wan, Lei1, Autor
Taschner, Michael2, Autor           
Cheng, Xi1, Autor
Lorentzen, Esben2, Autor           
Huang, Kaiyao1, Autor
Affiliations:
1external, ou_persistent22              
2Lorentzen, Esben / Intraflagellar Transport, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565157              

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Schlagwörter: CILIARY VESICLE DOCKING; CHLAMYDOMONAS-REINHARDTII; PRIMARY CILIUM; COMPLEX-B; CELLS ANTENNA; KINESIN-II; LOCALIZATION; DYNEIN; CORE; CILIOPATHIESCell Biology; Chlamydomonas; Intraflagellar transport; Basal body; Targeting sequence;
 Zusammenfassung: 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 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.

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Sprache(n): eng - English
 Datum: 2017
 Publikationsstatus: Erschienen
 Seiten: 13
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000402549400015
DOI: 10.1242/jcs.200758
 Art des Abschluß: -

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Titel: Journal of Cell Science
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Cambridge, U.K. : Co. of Biologists
Seiten: - Band / Heft: 130 (9) Artikelnummer: - Start- / Endseite: 1662 - 1674 Identifikator: ISSN: 0021-9533
CoNE: https://pure.mpg.de/cone/journals/resource/954925326678