A Repetitive Protein Essential for the Flagellum Attachment Zone Filament Structure and Function in Trypanosoma brucei

Vaughan, Sue; Kohl, Linda; Ngai, Ian; Wheeler, Richard J.; Gull, Keith

doi:10.1016/j.protis.2007.08.005

Cited by 122 publications

(186 citation statements)

References 24 publications

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“…8). Consistent with the importance of the FAZ in cytokinesis, RNAi knockdown of the FAZ proteins Fla-1 and FAZ1 lead to flagellum detachment and cytokinesis failure (LaCount et al, 2002;Vaughan et al, 2008).…”

Section: Cell Divisionmentioning

confidence: 66%

“…Flagellum adhesion glycoprotein 1 (Fla1), the T. brucei homolog of Trypanosoma cruzi GP72, localizes to the FAZ and is required for flagellum attachment (el-Sayed et al, 1995;Nozaki et al, 1996;LaCount et al, 2000LaCount et al, , 2002. Another FAZ component, FAZ1, was recently identified by screening an expression library with the monoclonal antibody L3B2 that recognizes the FAZ filament (Vaughan et al, 2008). FAZ1 is conserved amongst kinetoplastids and is required for normal FAZ assembly and flagellum attachment (Vaughan et al, 2008).…”

Section: Flagellum Attachment Zonementioning

confidence: 99%

“…Another FAZ component, FAZ1, was recently identified by screening an expression library with the monoclonal antibody L3B2 that recognizes the FAZ filament (Vaughan et al, 2008). FAZ1 is conserved amongst kinetoplastids and is required for normal FAZ assembly and flagellum attachment (Vaughan et al, 2008). Intriguingly, given the role of the FAZ in cytokinesis (see section 3.5), it is interesting that a T. brucei polo-like kinase homologue, TbPLK, has been localized to the FAZ (Kumar and Wang, 2006), although a separate study reported that TbPLK localizes to the cytoplasm (Hammarton et al, 2007).…”

Section: Flagellum Attachment Zonementioning

confidence: 99%

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The flagellum of Trypanosoma brucei: New tricks from an old dog

Ralston

Hill

2008

International Journal for Parasitology

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African trypanosomes, i.e. Trypanosoma brucei and related sub-species, are devastating human and animal pathogens that cause significant human mortality and limit sustained economic development in sub-Saharan Africa. Trypanosoma brucei is a highly motile protozoan parasite and coordinated motility is central to both disease pathogenesis in the mammalian host and parasite development in the tsetse fly vector. Since motility is critical for parasite development and pathogenesis, understanding unique aspects of the T. brucei flagellum may uncover novel targets for therapeutic intervention in African sleeping sickness. Moreover, studies of conserved features of the T. brucei flagellum are directly relevant to understanding fundamental aspects of flagellum and cilium function in other eukaryotes, making T. brucei an important model system. The T. brucei flagellum contains a canonical 9 + 2 axoneme, together with additional features that are unique to kinetoplastids and a few closely-related organisms. Until recently, much of our knowledge of the structure and function of the trypanosome flagellum was based on analogy and inference from other organisms. There has been an explosion in functional studies in T. brucei in recent years, revealing conserved as well as novel and unexpected structural and functional features of the flagellum. Most notably, the flagellum has been found to be an essential organelle, with critical roles in parasite motility, morphogenesis, cell division and immune evasion. This review highlights recent discoveries on the T. brucei flagellum.

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Section: Cell Divisionmentioning

confidence: 66%

Section: Flagellum Attachment Zonementioning

confidence: 99%

Section: Flagellum Attachment Zonementioning

confidence: 99%

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The flagellum of Trypanosoma brucei: New tricks from an old dog

Ralston

Hill

2008

International Journal for Parasitology

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“…The basal body is characterized by an array of nine microtubule triplets, with the conserved SAS-6 protein forming the cartwheel structure (10), similar to that of the centrosome in metazoa. The flagellum is attached, along most of its length, to the cell body via a specialized cytoskeletal structure termed the flagellum attachment zone (FAZ), 2 which consists of three main domains: the structure connecting the paraflagellar rod (PFR) to the flagellar membrane, the structure connecting the flagellar membrane and the cell body membrane, and a cytoplasmic filament (often referred to as the FAZ filament) and its associated microtubule quartet (11)(12)(13)(14)(15)(16)(17). In addition to mediating flagellum-cell body attachment, the FAZ filament also defines the cytokinesis cleavage plane (11,12), with the distal tip of the new FAZ filament marking the site of cytokinesis initiation (18 -20).…”

mentioning

confidence: 99%

SAS-4 Protein in Trypanosoma brucei Controls Life Cycle Transitions by Modulating the Length of the Flagellum Attachment Zone Filament

Zhou

2015

Journal of Biological Chemistry

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The centrosome in animals constitutes the cell's microtubule-organizing center that nucleates spindle assembly, and is characterized by a symmetrical array of nine microtubule triplets emanating from a cartwheel structure in the very proximal region of the centriole. Biogenesis of centrioles requires many regulatory proteins, including SAS-6, SAS-4/CPAP, and BLD10/CEP135, which are thought to constitute the core ancestral module involved in centriole assembly (1). The three proteins have distinct functions in centriole biogenesis. SAS-6 assembles to the cartwheel (2, 3) and BLD10/CEP135 forms the pinhead that connects the cartwheel spokes to the A-microtubules of the microtubule triplets (4, 5), whereas SAS-4/CPAP controls the elongation of centriolar microtubules (6 -9).Trypanosoma brucei, a flagellated protozoan and the causative agent of human sleeping sickness, does not have centrosomes, but it possesses the basal body as its microtubule-organizing center to nucleate the assembly of a motile flagellum. The basal body is characterized by an array of nine microtubule triplets, with the conserved SAS-6 protein forming the cartwheel structure (10), similar to that of the centrosome in metazoa. The flagellum is attached, along most of its length, to the cell body via a specialized cytoskeletal structure termed the flagellum attachment zone (FAZ), 2 which consists of three main domains: the structure connecting the paraflagellar rod (PFR) to the flagellar membrane, the structure connecting the flagellar membrane and the cell body membrane, and a cytoplasmic filament (often referred to as the FAZ filament) and its associated microtubule quartet (11)(12)(13)(14)(15)(16)(17). In addition to mediating flagellum-cell body attachment, the FAZ filament also defines the cytokinesis cleavage plane (11,12), with the distal tip of the new FAZ filament marking the site of cytokinesis initiation (18 -20). Moreover, during the cell cycle in the procyclic form, the elongation of the FAZ filament positions the newly assembled basal body toward the cell posterior (21), which is crucial for organelle segregation and cell division (10,(22)(23)(24)(25).Trypanosomatids, a group of kinetoplastid parasites consisting of T. brucei, Trypanosoma cruzi, and Leishmania spp., appear in a variety of different morphological forms during their life cycle and are distinguished by the relative position of the kinetoplast (mitochondrial DNA) and the nucleus and by the position, length, and cell body attachment of the flagellum (26). In the tsetse fly vector, T. brucei differentiates from the trypomastigote form to the epimastigote form, which undergoes asymmetrical cell division to produce a long epimastigote cell and a short epimastigote cell (26). How life cycle transitions in T. brucei are regulated is largely unknown, but recent work has begun to uncover the regulators involved in this process. ALBA3 and ALBA4, two closed related RNA-binding proteins, are the first factors found to be involved in life cycle transitions in T. brucei (27). Anothe...

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“…To examine whether flagellum detachment in SPBB1 RNAi cells was caused by defective assembly of the FAZ filament, cells were immunostained with the L3B2 antibody, which labels the FAZ1 protein in the FAZ filament (22,29), to monitor the integrity of the FAZ filament. In the non-induced control cells, all of the 2N2K cells contained two full-length FAZ filaments and two attached flagella.…”

Section: Spbb1 Co-localizes With Tbplk In the Basal Body During Earlymentioning

confidence: 99%

A Novel Basal Body Protein That Is a Polo-like Kinase Substrate Is Required for Basal Body Segregation and Flagellum Adhesion in Trypanosoma brucei

Hu¹,

Zhou²,

Li³

2015

Journal of Biological Chemistry

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Background:The substrates of Polo-like kinase in Trypanosoma brucei are mostly not identified. Results: A basal body protein was identified as a substrate of Polo-like kinase and is required for basal body segregation and flagellum adhesion. Conclusion: Polo-like kinase regulates a basal body protein.Significance: Dissecting the Polo-like kinase pathway is crucial for understanding its cellular functions.

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A Repetitive Protein Essential for the Flagellum Attachment Zone Filament Structure and Function in Trypanosoma brucei

Cited by 122 publications

References 24 publications

The flagellum of Trypanosoma brucei: New tricks from an old dog

The flagellum of Trypanosoma brucei: New tricks from an old dog

SAS-4 Protein in Trypanosoma brucei Controls Life Cycle Transitions by Modulating the Length of the Flagellum Attachment Zone Filament

A Novel Basal Body Protein That Is a Polo-like Kinase Substrate Is Required for Basal Body Segregation and Flagellum Adhesion in Trypanosoma brucei

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