Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei
| العنوان: | Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei |
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| المؤلفون: | Johannes Lesigang, Gang Dong, Mélanie Bonhivers, Marie Eggenspieler, Derrick R. Robinson, Keni Vidilaseris, Célia Florimond, Anna Albisetti, Nicolas Landrein |
| المساهمون: | Microbiologie cellulaire et moléculaire et pathogénicité (MCMP), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Shandong Academy of Agricultural Sciences (SAAS), Génomique fonctionnelle des trypanosomatides (GFT), Centre National de la Recherche Scientifique (CNRS), Université de Bordeaux (UB) |
| المصدر: | PLoS Pathogens PLoS Pathogens, Public Library of Science, 2017, 13 (11), pp.e1006710. ⟨10.1371/journal.ppat.1006710⟩ PLoS Pathogens, Vol 13, Iss 11, p e1006710 (2017) |
| بيانات النشر: | HAL CCSD, 2017. |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | 0301 basic medicine, [SDV]Life Sciences [q-bio], Immunofluorescence, Protozoan Proteins, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], Pathology and Laboratory Medicine, Microtubules, Biochemistry, RNA interference, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], Medicine and Health Sciences, Basal body, Biology (General), Cytoskeleton, ComputingMilieux_MISCELLANEOUS, Protozoans, Eukaryota, 3. Good health, Cell biology, Nucleic acids, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Genetic interference, Flagella, Epigenetics, Cellular Structures and Organelles, Pathogens, Research Article, Pathogen Motility, Trypanosoma, Virulence Factors, QH301-705.5, Trypanosoma brucei brucei, Immunology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Flagellum, Trypanosoma brucei, Research and Analysis Methods, Microbiology, [SDV.MP.PRO]Life Sciences [q-bio]/Microbiology and Parasitology/Protistology, Exocytosis, 03 medical and health sciences, Microtubule, Virology, Organelle, Trypanosoma Brucei, Genetics, Humans, [SDV.MP.PAR]Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Immunoassays, Molecular Biology, Organelles, 030102 biochemistry & molecular biology, Binding protein, Organisms, Biology and Life Sciences, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Cell Biology, RC581-607, biology.organism_classification, Parasitic Protozoans, Cytoskeletal Proteins, Kinetoplasts, 030104 developmental biology, Immunologic Techniques, RNA, Parasitology, Gene expression, Immunologic diseases. Allergy, Carrier Proteins, Biogenesis, Trypanosoma Brucei Gambiense |
| الوصف: | Trypanosoma brucei belongs to a group of unicellular, flagellated parasites that are responsible for human African trypanosomiasis. An essential aspect of parasite pathogenicity is cytoskeleton remodelling, which occurs during the life cycle of the parasite and is accompanied by major changes in morphology and organelle positioning. The flagellum originates from the basal bodies and exits the cell body through the flagellar pocket (FP) but remains attached to the cell body via the flagellum attachment zone (FAZ). The FP is an invagination of the pellicular membrane and is the sole site for endo- and exocytosis. The FAZ is a large complex of cytoskeletal proteins, plus an intracellular set of four specialised microtubules (MtQ) that elongate from the basal bodies to the anterior end of the cell. At the distal end of the FP, an essential, intracellular, cytoskeletal structure called the flagellar pocket collar (FPC) circumvents the flagellum. Overlapping the FPC is the hook complex (HC) (a sub-structure of the previously named bilobe) that is also essential and is thought to be involved in protein FP entry. BILBO1 is the only functionally characterised FPC protein and is necessary for FPC and FP biogenesis. Here, we used a combination of in vitro and in vivo approaches to identify and characterize a new BILBO1 partner protein—FPC4. We demonstrate that FPC4 localises to the FPC, the HC, and possibly to a proximal portion of the MtQ. We found that the C-terminal domain of FPC4 interacts with the BILBO1 N-terminal domain, and we identified the key amino acids required for this interaction. Interestingly, the FPC4 N-terminal domain was found to bind microtubules. Over-expression studies highlight the role of FPC4 in its association with the FPC, HC and FPC segregation. Our data suggest a tripartite association between the FPC, the HC and the MtQ. Author summary Trypanosoma brucei is the parasite responsible for human African trypanosomiasis, a disease also known as sleeping sickness. African trypanosomiasis is present in Sub-Saharan Africa and transmitted by infected tsetse flies. This devastating disease is lethal if untreated, making it important to understand and characterise the basic biology of the pathogen. During the T. brucei cell cycle, organelle positioning and segregation show a high degree of coordination and control. As such, T. brucei is a highly polarised cell with the transition zone of the flagellum present inside an invagination of the pellicular membrane called the flagellar pocket (FP). The FP is the main site of traffic into and out of the cell. At the exit point of the flagellum is a cytoskeletal structure called the flagellar pocket collar (FPC). One component of the FPC, BILBO1, has been characterised as essential for the FP biogenesis and cell survival. Here, we identify a new partner of BILBO1 called FPC4, and determine the domains involved in the BILBO1-FPC4 interaction. We further highlight the role of FPC4 in the segregation of the FPC and in the interplay between the FPC and other essential cytoskeletal structures. |
| اللغة: | English |
| تدمد: | 1553-7366 1553-7374 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e6061373b8a272f79e0a3dff5f21b33 https://hal.archives-ouvertes.fr/hal-02322324 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....3e6061373b8a272f79e0a3dff5f21b33 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15537366 15537374 |
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