A novel function for the atypical small G protein Rab-like 5 in the assembly of the trypanosome flagellum
| Autor: | Christine Adhiambo, Thierry Blisnick, Philippe Bastin, Géraldine Toutirais, Emmanuelle Delannoy |
|---|---|
| Přispěvatelé: | Biologie Cellulaire des Trypanosomes, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Molécules de Communication et Adaptation des Micro-organismes (MCAM), Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS), Régulation et dynamique des génomes, Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Blisnick, Thierry |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
MESH: Protein Transport
MESH: Mutation MESH: Sequence Homology Amino Acid Molecular Sequence Data Trypanosoma brucei brucei Protozoan Proteins MESH: Sequence Alignment Small G Protein MESH: Amino Acid Sequence MESH: Monomeric GTP-Binding Proteins Trypanosoma brucei Flagellum MESH: Flagella 03 medical and health sciences 0302 clinical medicine Intraflagellar transport MESH: Cilia [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN] Basal body Animals MESH: Animals MESH: Gene Silencing [SDV.MP.PAR]Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology Amino Acid Sequence Cilia Gene Silencing MESH: Protozoan Proteins Caenorhabditis elegans 030304 developmental biology Monomeric GTP-Binding Proteins 0303 health sciences MESH: Molecular Sequence Data biology Sequence Homology Amino Acid Cilium MESH: Trypanosoma brucei brucei Cell Biology biology.organism_classification Cell biology Protein Transport Flagella Mutation [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN] Rab sense organs Sequence Alignment 030217 neurology & neurosurgery [SDV.MP.PAR] Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology |
| Zdroj: | Journal of Cell Science Journal of Cell Science, Company of Biologists, 2009, 122 (6), pp.834-841. ⟨10.1242/jcs.040444⟩ Journal of Cell Science, 2009, 122 (6), pp.834-841. ⟨10.1242/jcs.040444⟩ |
| ISSN: | 0021-9533 1477-9137 |
| DOI: | 10.1242/jcs.040444⟩ |
| Popis: | International audience; The atypical small G protein Rab-like 5 has been shown to traffic in sensory cilia of Caenorhabditis elegans, where it participates in signalling processes but not in cilia construction. In this report, we demonstrate that RABL5 colocalises with intraflagellar transport (IFT) proteins at the basal body and in the flagellum matrix of the protist Trypanosoma brucei. RABL5 fused to GFP exhibits anterograde movement in the flagellum of live trypanosomes, suggesting it could be associated with IFT. Accordingly, RABL5 accumulates in the short flagella of the retrograde IFT140RNAi mutant and is restricted to the basal body region in the IFT88RNAi anterograde mutant, a behaviour that is identical to other IFT proteins. Strikingly, RNAi silencing reveals an essential role for RABL5 in trypanosome flagellum construction. RNAi knock-down produces a phenotype similar to inactivation of retrograde IFT with formation of short flagella that are filled with a high amount of IFT proteins. These data reveal for the first time a functional difference for a conserved flagellar matrix protein between two different ciliated species and raise questions related to cilia diversity. |
| Databáze: | OpenAIRE |
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