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

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Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly. / Wachter, Stefanie; Jung, Jamin; Shafiq, Shahaan; Basquin, Jerome; Fort, Cécile; Bastin, Philippe; Lorentzen, Esben.

I: EMBO Journal, Bind 38, Nr. 9, e101251, 05.2019.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Wachter, S, Jung, J, Shafiq, S, Basquin, J, Fort, C, Bastin, P & Lorentzen, E 2019, 'Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly', EMBO Journal, bind 38, nr. 9, e101251. https://doi.org/10.15252/embj.2018101251

APA

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

CBE

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

MLA

Vancouver

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

Author

Wachter, Stefanie ; Jung, Jamin ; Shafiq, Shahaan ; Basquin, Jerome ; Fort, Cécile ; Bastin, Philippe ; Lorentzen, Esben. / Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly. I: EMBO Journal. 2019 ; Bind 38, Nr. 9.

Bibtex

@article{bf56b59089884b18945f3fc1caf7d895,
title = "Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly",
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.",
keywords = "cilia, GTPase, IFT22, intraflagellar transport, Trypanosoma brucei",
author = "Stefanie Wachter and Jamin Jung and Shahaan Shafiq and Jerome Basquin and C{\'e}cile Fort and Philippe Bastin and Esben Lorentzen",
year = "2019",
month = may,
doi = "10.15252/embj.2018101251",
language = "English",
volume = "38",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell Publishing Ltd.",
number = "9",

}

RIS

TY - JOUR

T1 - Binding of IFT22 to the intraflagellar transport complex is essential for flagellum assembly

AU - Wachter, Stefanie

AU - Jung, Jamin

AU - Shafiq, Shahaan

AU - Basquin, Jerome

AU - Fort, Cécile

AU - Bastin, Philippe

AU - Lorentzen, Esben

PY - 2019/5

Y1 - 2019/5

N2 - 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.

AB - 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.

KW - cilia

KW - GTPase

KW - IFT22

KW - intraflagellar transport

KW - Trypanosoma brucei

UR - http://www.scopus.com/inward/record.url?scp=85063799499&partnerID=8YFLogxK

U2 - 10.15252/embj.2018101251

DO - 10.15252/embj.2018101251

M3 - Journal article

C2 - 30940671

AN - SCOPUS:85063799499

VL - 38

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 9

M1 - e101251

ER -