期刊
EMBO JOURNAL
卷 38, 期 9, 页码 -出版社
WILEY
DOI: 10.15252/embj.2018101251
关键词
cilia; GTPase; IFT22; intraflagellar transport; Trypanosoma brucei
资金
- Novo Nordisk Foundation [NNF15OC0014164]
- ANR [14-CE35-0009-01]
- French Government Investissement d'Avenir programme, Laboratoire d'Excellence Integrative Biology of Emerging Infectious Diseases [ANR-10-LABX-62-IBEID]
- La Fondation pour la Recherche Medicale [Equipe FRM DEQ20150734356, FDT20150532023]
- French National Ministry for Research and Technology [CDV515]
Intraflagellar transport (IFT) relies on motor proteins and the IFT complex to construct cilia and flagella. The IFT complex subunit IFT22/RabL5 has sequence similarity with small GTPases although the nucleotide specificity is unclear because of non-conserved G4/G5 motifs. We show that IFT22 specifically associates with G-nucleotides and present crystal structures of IFT22 in complex with GDP, GTP, and with IFT74/81. Our structural analysis unravels an unusual GTP/GDP-binding mode of IFT22 bypassing the classical G4 motif. The GTPase switch regions of IFT22 become ordered upon complex formation with IFT74/81 and mediate most of the IFT22-74/81 interactions. Structure-based mutagenesis reveals that association of IFT22 with the IFT complex is essential for flagellum construction in Trypanosoma brucei although IFT22 GTP-loading is not strictly required.
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