The Trypanosome Flagellar Pocket Collar and Its Ring Forming Protein—TbBILBO1

Perdomo, Doranda; Bonhivers, Mélanie; Robinson, Derrick R.

doi:10.3390/cells5010009

Cited by 19 publications

(22 citation statements)

References 103 publications

(165 reference statements)

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“…The flagellar pocket collar (FPC) and the hook complex (HC) are two essential T . brucei cytoskeletal structures whose molecular components are inadequately defined [ 29 , 50 ]. Furthermore, the molecular processes involved in their segregation during the cell cycle are poorly understood.…”

Section: Discussionmentioning

confidence: 99%

Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei

et al. 2017

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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.

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Section: Discussionmentioning

confidence: 99%

Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei

et al. 2017

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“…The trypanosomal FP, a membrane invagination surrounding the base of the flagellum, is a specialized organelle with multiple roles in the trypanosome [91,92]. This region is uniquely excluded from the sub-pellicular microtubule array under the parasites' plasma membrane [93,94]. The FP is also delineated from the rest of the plasma membrane by the FP collar, an electron-dense annulus, without which the FP is lost [93,95].…”

Section: Fishing From a Hole; The Flagellar Pocket And The Quest For mentioning

confidence: 99%

“…This region is uniquely excluded from the sub-pellicular microtubule array under the parasites' plasma membrane [93,94]. The FP is also delineated from the rest of the plasma membrane by the FP collar, an electron-dense annulus, without which the FP is lost [93,95]. This collar encloses the FP lumen, a space filled with a carbohydrate-rich matrix with a poorly defined composition and unknown function [91].…”

Section: Fishing From a Hole; The Flagellar Pocket And The Quest For mentioning

confidence: 99%

The Trypanosomal Transferrin Receptor of Trypanosoma Brucei—A Review

2019

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Iron is an essential element for life. Its uptake and utility requires a careful balancing with its toxic capacity, with mammals evolving a safe and bio-viable means of its transport and storage. This transport and storage is also utilized as part of the iron-sequestration arsenal employed by the mammalian hosts’ ‘nutritional immunity’ against parasites. Interestingly, a key element of iron transport, i.e., serum transferrin (Tf), is an essential growth factor for parasitic haemo-protozoans of the genus Trypanosoma. These are major mammalian parasites causing the diseases human African trypanosomosis (HAT) and animal trypanosomosis (AT). Using components of their well-characterized immune evasion system, bloodstream Trypanosoma brucei parasites adapt and scavenge for the mammalian host serum transferrin within their broad host range. The expression site associated genes (ESAG6 and 7) are utilized to construct a heterodimeric serum Tf binding complex which, within its niche in the flagellar pocket, and coupled to the trypanosomes’ fast endocytic rate, allows receptor-mediated acquisition of essential iron from their environment. This review summarizes current knowledge of the trypanosomal transferrin receptor (TfR), with emphasis on the structure and function of the receptor, both in physiological conditions as well as in conditions where the iron supply to parasites is being limited. Potential applications using current knowledge of the parasite receptor are also briefly discussed, primarily focused on potential therapeutic interventions.

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“…The flagellum is nucleated by a basal body that docks to the base of the flagellar pocket (FP), which is an invagination of the plasma membrane that functions as the sole site of endo-and exo-cytosis (Field and Carrington, 2009;Lacomble et al, 2009). The top of the FP is tightly apposed to the flagellar membrane by a series of cytoskeletal structures, including the flagella pocket collar, the hook complex and the centrin arm (Esson et al, 2012;Morriswood, 2015;Perdomo et al, 2016). Once the flagellum emerges onto the cell surface, it is attached to the cell body by the flagellum attachment zone (FAZ), which forms a series of desmosome-like structures that span the plasma and flagellar membranes to form a tight seal (Sunter and Gull, 2016;Vickerman, 1969).…”

Section: Introductionmentioning

confidence: 99%

Identification of TOEFAZ1‐interacting proteins reveals key regulators of Trypanosoma brucei cytokinesis

Hilton

Sladewski

Perry

et al. 2018

Molecular Microbiology

104

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The protist parasite Trypanosoma brucei is an obligate extracellular pathogen that retains its highly polarized morphology during cell division and has evolved a novel cytokinetic process independent of non-muscle myosin II. The polo-like kinase homolog TbPLK is essential for transmission of cell polarity during division and for cytokinesis. We previously identified a putative TbPLK substrate named Tip of the Extending FAZ 1 (TOEFAZ1) as an essential kinetoplastid-specific component of the T. brucei cytokinetic machinery. We performed a proximity-dependent biotinylation identification (BioID) screen using TOEFAZ1 as a means to identify additional proteins that are involved in cytokinesis. Using quantitative proteomic methods, we identified nearly 500 TOEFAZ1-proximal proteins and characterized 59 in further detail. Among the candidates, we identified an essential putative phosphatase that regulates the expression level and localization of both TOEFAZ1 and TbPLK, a previously uncharacterized protein that is necessary for the assembly of a new cell posterior, and a microtubule plus-end directed orphan kinesin that is required for completing cleavage furrow ingression. The identification of these proteins provides new insight into T. brucei cytokinesis and establishes TOEFAZ1 as a key component of this essential and uniquely configured process in kinetoplastids.

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The Trypanosome Flagellar Pocket Collar and Its Ring Forming Protein—TbBILBO1

Cited by 19 publications

References 103 publications

Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei

Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei

The Trypanosomal Transferrin Receptor of Trypanosoma Brucei—A Review

Identification of TOEFAZ1‐interacting proteins reveals key regulators of Trypanosoma brucei cytokinesis

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