Structure and division of the Golgi complex in Trichomonas vaginalis and Tritrichomonas foetus

Benchimol, Marlene; Ribeiro, Karla Consort; Mariante, Rafael M.; Alderete, John F.

doi:10.1078/0171-9335-00191

Cited by 48 publications

(27 citation statements)

References 47 publications

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“…Prior to mitosis, the T . vaginalis Golgi apparatus elongates and then divides through medial fission of each cisternae in a process called Golgikinesis, forming two Golgi ribbons [ 55 ]. We observed a similar pattern of staining adjacent to the nucleus in dividing cells where HA-TvROM2 ( Fig 1D and 1E ) and HA-TvROM3 localize, providing additional support for a Golgi localization of these proteins.…”

Section: Resultsmentioning

confidence: 99%

A Trichomonas vaginalis Rhomboid Protease and Its Substrate Modulate Parasite Attachment and Cytolysis of Host Cells

et al. 2015

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Trichomonas vaginalis is an extracellular eukaryotic parasite that causes the most common, non-viral sexually transmitted infection worldwide. Although disease burden is high, molecular mechanisms underlying T. vaginalis pathogenesis are poorly understood. Here, we identify a family of putative T. vaginalis rhomboid proteases and demonstrate catalytic activity for two, TvROM1 and TvROM3, using a heterologous cell cleavage assay. The two T. vaginalis intramembrane serine proteases display different subcellular localization and substrate specificities. TvROM1 is a cell surface membrane protein and cleaves atypical model rhomboid protease substrates, whereas TvROM3 appears to localize to the Golgi apparatus and recognizes a typical model substrate. To identify TvROM substrates, we interrogated the T. vaginalis surface proteome using both quantitative proteomic and bioinformatic approaches. Of the nine candidates identified, TVAG_166850 and TVAG_280090 were shown to be cleaved by TvROM1. Comparison of amino acid residues surrounding the predicted cleavage sites of TvROM1 substrates revealed a preference for small amino acids in the predicted transmembrane domain. Over-expression of TvROM1 increased attachment to and cytolysis of host ectocervical cells. Similarly, mutations that block the cleavage of a TvROM1 substrate lead to its accumulation on the cell surface and increased parasite adherence to host cells. Together, these data indicate a role for TvROM1 and its substrate(s) in modulating attachment to and lysis of host cells, which are key processes in T. vaginalis pathogenesis.

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Section: Resultsmentioning

confidence: 99%

A Trichomonas vaginalis Rhomboid Protease and Its Substrate Modulate Parasite Attachment and Cytolysis of Host Cells

et al. 2015

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“…The cisternae are polarized between the cisand trans-sides within a stack, and glycosylation enzymes localize sequentially from cis to trans in the order in which they function (Dunphy and Rothman, 1985;Glick and Luini, 2011). Knowledge about what occurs during the biogenesis of this structure is limited to research on a few protozoanstypically organisms with only one Golgi stack per cellyet these results have proposed a variety of schemes for Golgi generation (Benchimol et al, 2001;Bevis et al, 2002;He et al, 2004;Pelletier et al, 2002). Molecular mechanisms that govern Golgi formation remain to be unveiled.…”

Section: Introductionmentioning

confidence: 99%

The Golgi entry core compartment functions as a COPII-independent scaffold for ER-to-Golgi transport in plant cells

Ito

Uemura

Nakano

2018

Journal of Cell Science

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Many questions remain about how the stacked structure of the Golgi is formed and maintained. In our previous study, we challenged this question using tobacco BY-2 cells and revealed that, upon Brefeldin A (BFA) treatment, previously undescribed small punctate structures containing a particular subset of -Golgi proteins are formed adjacent to the ER-exit sites and act as scaffolds for Golgi regeneration after BFA removal. In this study, we analyzed these structures further. The proteins that localize to these punctate structures originate from the-most cisternae. 3D time-lapse observations show that the -Golgi marker is transported through these structures during Golgi regeneration. These data indicate that the-most cisternae have a specialized region that receives cargo from the ER, which becomes obvious upon BFA treatment. Expression of a dominant mutant form of SAR1 does not affect the formation of the punctate structures. We propose to call these punctate structures the 'Golgi entry core compartment' (GECCO). They act as receivers for the rest of the Golgi materials and are formed independently of the COPII machinery.This article has an associated First Person interview with the first author of the paper.

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“…The first model is templated biogenesis, in which the old Golgi is thought to act as a scaffold for the new. This model has its origins in EM images that appear to show elongated Golgi stacks dividing into two ( Domozych et al, 1981 ; Benchimol et al, 2001 ). Though static images cannot indicate the direction of events, we have recently been able to confirm this sequence by exploiting the simplicity of the protozoan parasite Toxoplasma gondii and its amenability to genetic manipulation.…”

Section: Introductionmentioning

confidence: 99%

Golgi duplication in Trypanosoma brucei

Malsam

et al. 2004

The Journal of Cell Biology

155

145

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Duplication of the single Golgi apparatus in the protozoan parasite Trypanosoma brucei has been followed by tagging a putative Golgi enzyme and a matrix protein with variants of GFP. Video microscopy shows that the new Golgi appears de novo, near to the old Golgi, about two hours into the cell cycle and grows over a two-hour period until it is the same size as the old Golgi. Duplication of the endoplasmic reticulum (ER) export site follows exactly the same time course. Photobleaching experiments show that the new Golgi is not the exclusive product of the new ER export site. Rather, it is supplied, at least in part, by material directly from the old Golgi. Pharmacological experiments show that the site of the new Golgi and ER export is determined by the location of the new basal body.

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Structure and division of the Golgi complex in Trichomonas vaginalis and Tritrichomonas foetus

Cited by 48 publications

References 47 publications

A Trichomonas vaginalis Rhomboid Protease and Its Substrate Modulate Parasite Attachment and Cytolysis of Host Cells

A Trichomonas vaginalis Rhomboid Protease and Its Substrate Modulate Parasite Attachment and Cytolysis of Host Cells

The Golgi entry core compartment functions as a COPII-independent scaffold for ER-to-Golgi transport in plant cells

Golgi duplication in Trypanosoma brucei

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