English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly

MPS-Authors
/persons/resource/persons195442

Wachter,  Stefanie
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77713

Basquin,  Jerome
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

Fulltext (public)

embj.2018101251.pdf
(Publisher version), 9MB

Supplementary Material (public)

embj2018101251-sup-0001-appendix.pdf
(Supplementary material), 2MB

Citation

Wachter, S., Jung, J., Shafiq, S., Basquin, J., Fort, C., Bastin, P., et al. (2019). Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly. EMBO Journal, 38(9): e101251. doi:10.15252/embj.2018101251.


Cite as: http://hdl.handle.net/21.11116/0000-0003-E7ED-E
Abstract
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.