Kinesin 9 family members perform separate functions in the trypanosome flagellum

Demonchy, Raphaël; Blisnick, Thierry; Deprez, Caroline; Toutirais, Géraldine; Loussert, Céline; Marande, William; Grellier, Philippe; Bastin, Philippe; Kohl, Linda

doi:10.1083/jcb.200903139

Cited by 60 publications

(87 citation statements)

References 39 publications

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“…This process emerges relatively late (2-3 days after RNAi induction), possibly either because of slow displacement of KIF9B or because only a proportion of KIF9B is motile. This is compatible with the absence of GFP::KIF9B movement in short video acquisitions (Demonchy et al, 2009).…”

Section: Ift and The Maintenance Of Flagellar Componentssupporting

confidence: 82%

“…We next investigated the location of the KIF9B protein, a kinesin molecular motor involved in the assembly of the PFR that is present along the axoneme and at the base of both old and new flagella (Demonchy et al, 2009). IFT88…”

Section: Ift Is Required For the Correct Distribution Of Non-skeletalmentioning

confidence: 99%

“…In the absence of KIF9B, trypanosomes assemble an apparently normal axoneme but the construction of the PFR is defective: large 'blocks' of PFR materials alternate with regions where only the axoneme is present (Demonchy et al, 2009). It has been suggested that the motor activity of KIF9B somehow contributes to the transport of PFR proteins during construction of the structure.…”

Section: Ift and The Maintenance Of Flagellar Componentsmentioning

confidence: 99%

“…The vector was linearized by EcoRI and integrated in the hydin endogenous locus, resulting in a reconstructed complete eGFP::Hydin fusion. Plasmids p2675YFPIFT81 (Bhogaraju et al, 2013), pPCPFReGFPKIF9B (Demonchy et al, 2009) and p3329FLAM8 (Subota et al, 2014) have been described previously.…”

Section: Plasmid Construction and Transformation In Trypanosomesmentioning

confidence: 99%

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Intraflagellar transport is required for the maintenance of the trypanosome flagellum composition but not its length

Fort

Bonnefoy

Kohl

et al. 2016

Journal of Cell Science

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Intraflagellar transport (IFT) is required for construction of most cilia and flagella. Here, we used electron microscopy, immunofluorescence and live video microscopy to show that IFT is absent or arrested in the mature flagellum of Trypanosoma brucei upon RNA interference (RNAi)-mediated knockdown of IFT88 and IFT140, respectively. Flagella assembled prior to RNAi did not shorten, showing that IFT is not essential for the maintenance of flagella length. Although the ultrastructure of the axoneme was not visibly affected, flagellar beating was strongly reduced and the distribution of several flagellar components was drastically modified. The R subunit of the protein kinase A was no longer concentrated in the flagellum but was largely found in the cell body whereas the kinesin 9B motor was accumulating at the distal tip of the flagellum. In contrast, the distal tip protein FLAM8 was dispersed along the flagellum. This reveals that IFT also functions in maintaining the distribution of some flagellar proteins after construction of the organelle is completed.

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Section: Ift and The Maintenance Of Flagellar Componentssupporting

confidence: 82%

Section: Ift Is Required For the Correct Distribution Of Non-skeletalmentioning

confidence: 99%

Section: Ift and The Maintenance Of Flagellar Componentsmentioning

confidence: 99%

Section: Plasmid Construction and Transformation In Trypanosomesmentioning

confidence: 99%

See 2 more Smart Citations

Intraflagellar transport is required for the maintenance of the trypanosome flagellum composition but not its length

Fort

Bonnefoy

Kohl

et al. 2016

Journal of Cell Science

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“…However, a rudimentary PFR is still assembled in these mutants (Bastin et al, 1998). We next investigated FLAM3::YFP distribution in the KIF9B RNAi mutants that exhibit some flagellum regions with only the axoneme and others with massive blocks of PFR material (Demonchy et al, 2009). Here too, FLAM3::YFP localized normally to the axoneme along the entire flagellum (Fig.…”

Section: Targeting Of Fla1 and Flam3 To The Faz Is Independent Of Flamentioning

confidence: 97%

Flagellar adhesion inTrypanosoma bruceirelies on interactions between different skeletal structures present in the flagellum and in the cell body

Rotureau

Blisnick

Subota

et al. 2013

Journal of Cell Science

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The Trypanosoma brucei flagellum is an essential organelle anchored along the surface of the cell body through a specialized structure called the flagellum attachment zone (FAZ). Adhesion relies on the interaction of the extracellular portion of two transmembrane proteins, FLA1 and FLA1BP. Here, we identify FLAM3 as a novel large protein associated with the flagellum skeleton whose ablation inhibits flagellum attachment. FLAM3 does not contain transmembrane domains and its flagellar localization matches closely, but not exactly, that of the paraflagellar rod, an extraaxonemal structure present in the flagellum. Knockdown of FLA1 or FLAM3 triggers similar defects in motility and morphogenesis, characterized by the assembly of a drastically reduced FAZ filament. FLAM3 remains associated with the flagellum skeleton even in the absence of adhesion or a normal paraflagellar rod. However, the protein is dispersed in the cytoplasm when flagellum formation is inhibited. By contrast, FLA1 remains tightly associated with the FAZ filament even in the absence of a flagellum. In these conditions, the extracellular domain of FLA1 points to the cell surface. FLAM3 is essential for proper distribution of FLA1BP, which is restricted to the most proximal portion of the flagellum upon knockdown of FLAM3. We propose that FLAM3 is a key component of the FAZ connectors that link the axoneme to the adhesion zone, hence it acts in an equivalent manner to the FAZ filament complex, but on the side of the flagellum.

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Restriction of intraflagellar transport to some microtubule doublets: An opportunity for cilia diversification?

Mallet

Bastin

2022

BioEssays

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Cilia are unique eukaryotic organelles and exhibit remarkable conservation across evolution. Nevertheless, very different types of configurations are encountered, raising the question of their evolution. Cilia are constructed by intraflagellar transport (IFT), the movement of large protein complexes or trains that deliver cilia components to the distal tip for assembly. Recent data revealed that IFT trains are restricted to some but not all nine doublet microtubules in the protist Trypanosoma brucei. Here, we propose that restricted positioning of IFT trains could offer potent options for cilia to evolve towards more complex (addition of new structural elements like in spermatozoa) or simpler configuration (loss of some elements like in primary cilia), and therefore be a driver of cilia diversification. We present two hypotheses to explain how IFT trains could be restricted to some doublets, either by a triage process taking place at the basal body level or by the development of molecular differences between ciliary microtubules.

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Kinesin 9 family members perform separate functions in the trypanosome flagellum

Abstract: KIF9B localizes to the axoneme and basal body and is needed for flagella assembly, whereas KIF9A localizes only to the axoneme and controls flagella motility without affecting their structure.

Cited by 60 publications

References 39 publications

Intraflagellar transport is required for the maintenance of the trypanosome flagellum composition but not its length

Intraflagellar transport is required for the maintenance of the trypanosome flagellum composition but not its length

Flagellar adhesion inTrypanosoma bruceirelies on interactions between different skeletal structures present in the flagellum and in the cell body

Restriction of intraflagellar transport to some microtubule doublets: An opportunity for cilia diversification?

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