The bilobe structure of Trypanosoma brucei contains a MORN-repeat protein

Morriswood, Brooke; He, Cynthia Y.; Sealey‐Cardona, Marco; Yelinek, Jordan T.; Pypaert, Marc; Warren, Graham

doi:10.1016/j.molbiopara.2009.05.001

Cited by 55 publications

(124 citation statements)

References 40 publications

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“…This result was therefore consistent with the partial overlap between the bi-lobe and the FAZ previously observed by light microscopy (supplementary material Fig. S2J-L) (Shi et al, 2008;Morriswood et al, 2009;Zhou et al, 2010).…”

Section: T Brucei Cc2dsupporting

confidence: 91%

“…Inhibited flagellum formation in intraflagellar transport mutants results in truncated FAZ (Absalon et al, 2007;Kohl et al, 2003). Furthermore, our previous work suggests a possible link between the FAZ filament and the Golgiadjacent bi-lobed structure, which plays a crucial role in organelle biogenesis and cell division (Morriswood et al, 2009;Shi et al, 2008;Zhou et al, 2010). The centrally located bi-lobe overlaps with the posterior tip of the FAZ and duplication of the bi-lobe is immediately followed by formation of a new FAZ.…”

Section: Introductionmentioning

confidence: 91%

“…For endogenous replacement, 500 bp of 59-untranslated region and 500 bp of the 59-end coding sequence of CC2D were PCR-amplified and then cloned separately into a modified pCR4Blunt-TOPO vector flanking a YFP-or Ty-tagging cassette (Morriswood et al, 2009). For RNAi studies, the RNAit program (Redmond et al, 2003) was used for the identification of suitable RNAi fragment.…”

Section: Plasmid Construction and Transfectionmentioning

confidence: 99%

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A coiled-coil- and C2-domain-containing protein is required for FAZ assembly and cell morphology in Trypanosoma brucei

Zhou

Liu

Sun

et al. 2011

Journal of Cell Science

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150

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SummaryTrypanosoma brucei, a flagellated protozoan parasite causing human sleeping sickness, relies on a subpellicular microtubule array for maintenance of cell morphology. The flagellum is attached to the cell body through a poorly understood flagellum attachment zone (FAZ), and regulates cell morphogenesis using an unknown mechanism. Here we identified a new FAZ component, CC2D, which contains coiled-coil motifs followed by a C-terminal C2 domain. T. brucei CC2D is present on the FAZ filament, FAZ-juxtaposed ER membrane and the basal bodies. Depletion of CC2D inhibits the assembly of a new FAZ filament, forming a FAZ stub with a relatively fixed size at the base of a detached, but otherwise normal, flagellum. Inhibition of new FAZ formation perturbs subpellicular microtubule organization and generates short daughter cells. The cell length shows a strong linear correlation with FAZ length, in both control cells and in cells with inhibited FAZ assembly. Together, our data support a direct function of FAZ assembly in determining new daughter cell length by regulating subpellicular microtubule synthesis.

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Section: T Brucei Cc2dsupporting

confidence: 91%

Section: Introductionmentioning

confidence: 91%

Section: Plasmid Construction and Transfectionmentioning

confidence: 99%

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A coiled-coil- and C2-domain-containing protein is required for FAZ assembly and cell morphology in Trypanosoma brucei

Zhou

Liu

Sun

et al. 2011

Journal of Cell Science

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150

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“…The cells were stained with primary antibody (anti-TbPLK diluted 1:50, anti-FAZ1 1:200, anti-BILBO1 1:8, anti-C4 1:80, anti-C2 1:30 or anti-TBBC 1:800) washed in PBS, then stained with secondary antibodies. The cells were washed in PBS, mounted in DAPI Fluormount G (Southern Biotech), and visualized as previously described (Morriswood et al, 2009). …”

Section: Immunofluorescencementioning

confidence: 99%

“…The flagellar pocket collar (FPC), a structure comprising the protein BILBO1, tightly clinches the neck of the flagellar pocket against the flagellum, which limits access to the compartment Gadelha et al, 2009). The neck of the flagellar pocket is also partially encircled by the hook-like extension of a MORN1-containing cytoskeletal complex, the stem of which coincides with the posterior part of the FAZ (Morriswood et al, 2009). This MORN1 complex is part of a larger cytoskeletal structure termed the bilobe, which also contains small calcium-binding proteins called centrins and a leucine-rich repeat protein known as TbLRRP1 (Broadhead et al, 2006;Shi et al, 2008;Selvapandiyan et al, 2007;He et al, 2005;Zhou et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Polo-like kinase is necessary for flagellum inheritance in Trypanosoma brucei

Ikeda¹,

Graffenried²

2012

Journal of Cell Science

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SummaryPolo-like kinases play an important role in a variety of mitotic events in mammalian cells, ranging from centriole separation and chromosome congression to abscission. To fulfill these roles, Polo-like kinase homologs move to different cellular locations as the cell cycle progresses, starting at the centrosome, progressing to the spindle poles and then the midbody. In the protist parasite Trypanosoma brucei, the single polo-like kinase homolog T. brucei PLK (TbPLK) is essential for cytokinesis and is necessary for the correct duplication of a centrin-containing cytoskeletal structure known as the bilobe. We show that TbPLK has a dynamic localization pattern during the cell cycle. The kinase localizes to the basal body, which nucleates the flagellum, and then successively localizes to a series of cytoskeletal structures that regulate the position and attachment of the flagellum to the cell body. The kinase localizes to each of these structures as they are duplicating. TbPLK associates with a specialized set of microtubules, known as the microtubule quartet, which might transport the kinase during its migration. Depletion of TbPLK causes defects in basal body segregation and blocks the duplication of the regulators that position the flagellum, suggesting that its presence on these structures might be necessary for their proper biogenesis. TbPLK migrates throughout the cell in T. brucei, but the specific locations to which it targets and its functions are geared towards the inheritance of a properly positioned and attached flagellum.

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Proteomic Analyses of a Bi-Lobed Structure in Trypanosoma brucei

Gheiratmand

2014

Membrane Trafficking

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The position and function of the Golgi apparatus are tightly coupled with the microtubule-organizing centers (MTOCs) that play important roles in cell growth and polarity. In the unicellular parasite Trypanosoma brucei, the single Golgi apparatus is adjacent to a novel, bilobed structure located at the proximal base of the flagellum, near to the basal body that nucleates the flagellar axoneme. The duplication and segregation of the bilobed structure are tightly coupled to the duplication and segregation of Golgi, ER exit site, basal bodies, and flagellum, suggesting a role of this unique structure in the precise positioning, biogenesis, and inheritance of these single-copied structures during the cell cycle of procyclic T. brucei. Here, we describe in details two different isolation and proteomic methods to characterize the protein components present on or associated with the bilobed structure, which allow further understanding of its function and association with other membranous and cytoskeletal organelles in the parasite.

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The bilobe structure of Trypanosoma brucei contains a MORN-repeat protein

Cited by 55 publications

References 40 publications

A coiled-coil- and C2-domain-containing protein is required for FAZ assembly and cell morphology in Trypanosoma brucei

A coiled-coil- and C2-domain-containing protein is required for FAZ assembly and cell morphology in Trypanosoma brucei

Polo-like kinase is necessary for flagellum inheritance in Trypanosoma brucei

Proteomic Analyses of a Bi-Lobed Structure in Trypanosoma brucei

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