TbG63, a golgin involved in Golgi architecture in<i>Trypanosoma brucei</i>

Ramirez, Irene Barinaga-Rementeria; Graffenried, Christopher L. de; Ebersberger, Ingo; Yelinek, Jordan T.; He, Cynthia Y.; Price, Albert; Warren, Graham

doi:10.1242/jcs.014324

Cited by 12 publications

(20 citation statements)

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“…To confirm the lack of basal bodies and bi-lobed structures, the purified flagella fraction was fixed and labeled with an antibody against TbCentrin4, which stains both the basal bodies and the bi-lobed structure [10]. While TbCentrin4 labeling was readily identifiable at the tip of each flagellum in the extracted flagellar complex, no TbCentrin4 staining was detected in the detached flagella fraction (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…For labeling with anti-TbMORN1, the cells were extracted with 0.5% Nonidet P-40 in PEM, fixed with 4% paraformaldehyde and then processed for antibody labeling. Anti-TbGRASP [3], L3B2 [24], YL1/2 [25], anti-TbBILBO1 [4], anti-TbMORN1 [12], and anti-TbCentrin4 [10] were used to label the Golgi, the FAZ, the basal bodies, the FPC and the bi-lobed structure, respectively. DAPI (2 µg/ml) was used to stain kinetoplast and nuclear DNA.…”

Section: Methodsmentioning

confidence: 99%

“…Both TbCentrin2 and TbCentrin4 (also known as TbCen1 [9]) are found localized to both the bi-lobed structure and the basal bodies in T. brucei . While depletion of TbCentrin2 inhibits the duplication/segregation of basal bodies, Golgi, kinetoplast, FAZ and final cell division, depletion of TbCentrin4 did not affect the duplication of organelles, but did disrupt the timing between nuclear division and the subsequent cytokinesis through an unknown mechanism [10].…”

Section: Introductionmentioning

confidence: 95%

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A Comparative Proteomic Analysis Reveals a New Bi-Lobe Protein Required for Bi-Lobe Duplication and Cell Division in Trypanosoma brucei

et al. 2010

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A Golgi-associated bi-lobed structure was previously found to be important for Golgi duplication and cell division in Trypanosoma brucei. To further understand its functions, comparative proteomics was performed on extracted flagellar complexes (including the flagellum and flagellum-associated structures such as the basal bodies and the bi-lobe) and purified flagella to identify new bi-lobe proteins. A leucine-rich repeats containing protein, TbLRRP1, was characterized as a new bi-lobe component. The anterior part of the TbLRRP1-labeled bi-lobe is adjacent to the single Golgi apparatus, and the posterior side is tightly associated with the flagellar pocket collar marked by TbBILBO1. Inducible depletion of TbLRRP1 by RNA interference inhibited duplication of the bi-lobe as well as the adjacent Golgi apparatus and flagellar pocket collar. Formation of a new flagellum attachment zone and subsequent cell division were also inhibited, suggesting a central role of bi-lobe in Golgi, flagellar pocket collar and flagellum attachment zone biogenesis.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 95%

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A Comparative Proteomic Analysis Reveals a New Bi-Lobe Protein Required for Bi-Lobe Duplication and Cell Division in Trypanosoma brucei

et al. 2010

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“…TbG63 is involved in the Golgi architecture or the growth of the parasites in the bloodstream (Ramirez et al 2008). The Drosophila Lava lamp is a novel golgin that is required for cellularization by promoting dynein-based Golgi motility (Papoulas et al 2005).…”

Section: Golgins In Yeast Plants and Other Speciesmentioning

confidence: 99%

New components of the Golgi matrix

Xiang

Wang

2011

Cell Tissue Res

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The eukaryotic Golgi apparatus is characterized by a stack of flattened cisternae that are surrounded by transport vesicles. The organization and function of the Golgi require Golgi matrix proteins, including GRASPs and golgins, which exist primarily as fiber-like bridges between Golgi cisternae or between cisternae and vesicles. In this review, we highlight recent findings on Golgi matrix proteins, including their roles in maintaining the Golgi structure, vesicle tethering, and novel, unexpected functions. These new discoveries further our understanding of the molecular mechanisms that maintain the structure and the function of the Golgi, as well as its relationship with other cellular organelles such as the centrosome.

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“…Golgins are characterized by their predicted, highly extended, coiled-coil structures, and they typically have a high glutamic acid content (Ramirez et al, 2008). Certain Golgins have been implicated as transport vesicle tethers that help capture vesicles and bring them closer to their cognate targets; they are also essential for the maintenance of normal Golgi structure.…”

Section: Introductionmentioning

confidence: 99%

Multiple Rab GTPase Binding Sites in GCC185 Suggest a Model for Vesicle Tethering at theTrans-Golgi

Hayes

Brown

Haas

et al. 2009

MBoC

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GCC185, a trans-Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose 6-phosphate receptors (MPRs) to the Golgi and for microtubule nucleation at the Golgi via CLASP proteins. GCC185 localizes to the Golgi by cooperative interaction with Rab6 and Arl1 GTPases at adjacent sites near its C terminus. We show here by yeast two-hybrid and direct biochemical tests that GCC185 contains at least four additional binding sites for as many as 14 different Rab GTPases across its entire length. A central coiled-coil domain contains a specific Rab9 binding site, and functional assays indicate that this domain is important for MPR recycling to the Golgi complex. N-Terminal coiled-coils are also required for GCC185 function as determined by plasmid rescue after GCC185 depletion by using small interfering RNA in cultured cells. Golgi-Rab binding sites may permit GCC185 to contribute to stacking and lateral interactions of Golgi cisternae as well as help it function as a vesicle tether. INTRODUCTIONThe Golgi complex plays a central role in processing and sorting of secreted and membrane proteins. In mammalian cells, it is made up of a set of flattened cisternae that are organized as a stack (Farquhar and Palade, 1998). Within the Golgi, proteins undergo oligosaccharide side chain maturation, and they are sorted to different destinations, including apical or basolateral plasma membranes, prelysosomes, or secretory storage granules, as they exit this compartment.The Golgi surface is decorated with proteins called Golgins (Short et al., 2005;Sztul and Lupashin, 2006). Golgins are characterized by their predicted, highly extended, coiled-coil structures, and they typically have a high glutamic acid content (Ramirez et al., 2008). Certain Golgins have been implicated as transport vesicle tethers that help capture vesicles and bring them closer to their cognate targets; they are also essential for the maintenance of normal Golgi structure. For example, temperature-sensitive cells lacking GM130 have a disrupted Golgi at the nonpermissive temperature (Vasile et al., 2003); loss of Golgin-84 (Diao et al., 2003), Golgin-245 (Yoshino et al., 2005), TATA modulatory factor (Fridmann-Sirkis et al., 2004), GRASP55 (Feinstein and Linstedt, 2008), GRASP65 (Puthenveedu et al., 2006), and the so-called COG complex (Zolov and Lupashin, 2005) all lead to disruption of the Golgi ribbon. Thus, the Golgi complex is highly sensitive to the loss of any one of a large collection of Golgi-associated proteins.Most Golgins are peripherally associated with this organelle by virtue of interaction with small GTPases of the Rab and/or Arf (Arl) families; a few contain C-terminal membrane anchors (Short et al., 2005). Four human Golgins contain a so-called GRIP domain at their C termini that enables them to bind the Arl1 GTPase at the trans-Golgi network (TGN); Arl1 is essential for the Golgi targeting of multiple GRIP domain-containing proteins (Lu and Hong, 2003;Panic et al., 2003...

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TbG63, a golgin involved in Golgi architecture inTrypanosoma brucei

Cited by 12 publications

References 44 publications

A Comparative Proteomic Analysis Reveals a New Bi-Lobe Protein Required for Bi-Lobe Duplication and Cell Division in Trypanosoma brucei

A Comparative Proteomic Analysis Reveals a New Bi-Lobe Protein Required for Bi-Lobe Duplication and Cell Division in Trypanosoma brucei

New components of the Golgi matrix

Multiple Rab GTPase Binding Sites in GCC185 Suggest a Model for Vesicle Tethering at theTrans-Golgi

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