Targeted proteomic dissection of <i>Toxoplasma</i> cytoskeleton sub‐compartments using MORN1

Lorestani, Alexander; Ivey, F. Douglas; Thirugnanam, Sivasakthivel; Busby, Michele; Marth, Gábor; Cheeseman, Iain M.; Gubbels, Marc‐Jan

doi:10.1002/cm.21077

Cited by 50 publications

(61 citation statements)

References 61 publications

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“…In dividing parasites, TgDrpC always relocated from cytoplasm to ring like structures at the growing ends of the daughter buds. This localization parallels that of MORN1, a scaffolding protein essential in assembling the basal complex (Lorestani et al , ). Besides MORN1, the basal complex includes the centrin protein TgCen2 and the alveolin motif containing proteins IMC5, IMC8, IMC9 and IMC 13 (Hu, ; Anderson‐White et al , ; Lorestani et al , ).…”

Section: Discussionsupporting

confidence: 58%

“…This localization parallels that of MORN1, a scaffolding protein essential in assembling the basal complex (Lorestani et al , ). Besides MORN1, the basal complex includes the centrin protein TgCen2 and the alveolin motif containing proteins IMC5, IMC8, IMC9 and IMC 13 (Hu, ; Anderson‐White et al , ; Lorestani et al , ). In dividing parasites, the complex is assembled with the rest of the new cytoskeleton, forming a ring‐like structure at the growing edge of the daughter cells.…”

Section: Discussionsupporting

confidence: 58%

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TgDrpC, an atypical dynamin‐related protein in Toxoplasma gondii, is associated with vesicular transport factors and parasite division

Heredero‐Bermejo

Varberg

Charvat

et al. 2018

Molecular Microbiology

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Summary Dynamin-related proteins (Drps) are involved in diverse processes such as organelle division and vesicle trafficking. The intracellular parasite Toxoplasma gondii possesses three distinct Drps. TgDrpC, whose function remains unresolved, is unusual in that it lacks a conserved GTPase Effector Domain, which is typically required for function. Here, we show that TgDrpC localizes to cytoplasmic puncta; however, in dividing parasites, TgDrpC redistributes to the growing edge of the daughter cells. By conditional knockdown, we determined that loss of TgDrpC stalls division and leads to rapid deterioration of multiple organelles and the IMC. We also show that TgDrpC interacts with proteins that exhibit homology to those involved in vesicle transport, including members of the adaptor complex 2. Two of these proteins, a homolog of the adaptor protein 2 (AP-2) complex subunit alpha-1 and a homolog of the ezrin–radixin–moesin (ERM) family proteins, localize to puncta and associate with the daughter cells. Consistent with the association with vesicle transport proteins, re-distribution of TgDrpC to the IMC during division is dependent on post-Golgi trafficking. Together, these results support that TgDrpC contributes to vesicle trafficking and is critical for stability of parasite organelles and division.

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Section: Discussionsupporting

confidence: 58%

Section: Discussionsupporting

confidence: 58%

TgDrpC, an atypical dynamin‐related protein in Toxoplasma gondii, is associated with vesicular transport factors and parasite division

Heredero‐Bermejo

Varberg

Charvat

et al. 2018

Molecular Microbiology

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“…Toxoplasma flagella are restricted to male gametes, and a number of conserved centriole and flagellar components were apparently lost from the apicomplexan lineage (50). Nonetheless, the centriole serves as a signaling platform, with novel parasite-specific proteins that move from it to developing daughter buds during Toxoplasma zoite replication (81,89,105). Moreover, although zoites lack flagella, they retain several flagellar apparatus-associated proteins which may be important for diverse processes, including replication and invasion (87)(88)(89).…”

Section: Discussionmentioning

confidence: 99%

“…Following centriole separation, several centriole-associated proteins relocate to emerging daughters. RNG2 shifts from the centrioles to the APR (89), and both IMC15 and Tg14-3-3 move from the centrioles to the IMC of emergent daughters (81,105). Although the timing of bud formation in endodyogeny versus that in endopolygeny is distinct, the cytoskeletal components are likely to be quite similar, with assembly regulated by initiation of key structures, such as the conoid, APR, IMC, and underlying microtubules (69,127).…”

Section: Microtubule-dependent Processesmentioning

confidence: 99%

Targeting Toxoplasma Tubules: Tubulin, Microtubules, and Associated Proteins in a Human Pathogen

Morrissette

2015

Eukaryot Cell

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Toxoplasma gondii is an obligate intracellular parasite that causes serious opportunistic infections, birth defects, and blindness in humans. Microtubules are critically important components of diverse structures that are used throughout the Toxoplasma life cycle. As in other eukaryotes, spindle microtubules are required for chromosome segregation during replication. Additionally, a set of membrane-associated microtubules is essential for the elongated shape of invasive "zoites," and motility follows a spiral trajectory that reflects the path of these microtubules. Toxoplasma zoites also construct an intricate, tubulin-based apical structure, termed the conoid, which is important for host cell invasion and associates with proteins typically found in the flagellar apparatus. Last, microgametes specifically construct a microtubule-containing flagellar axoneme in order to fertilize macrogametes, permitting genetic recombination. The specialized roles of these microtubule populations are mediated by distinct sets of associated proteins. This review summarizes our current understanding of the role of tubulin, microtubule populations, and associated proteins in Toxoplasma; these components are used for both novel and broadly conserved processes that are essential for parasite survival.

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“…Interestingly, TgMORN1, which also localises to the basal complex, plays a key role in cell shape integrity during daughter cells biogenesis35. However, there is so far no evidence of a direct TgDIP13/TgMORN1 interaction, as TgDIP13 was not found in co-immunoprecipitation36 or two-hybrid37 analyses of TgMORN1 binding partners. A variety of appendages and accessory structures associated with MTOCs are performing roles in the orchestration of cell architecture, and in defining MTOC connections for biogenesis and inheritance.…”

Section: Discussionmentioning

confidence: 99%

An evolutionarily conserved SSNA1/DIP13 homologue is a component of both basal and apical complexes of Toxoplasma gondii

Lévêque

Berry

Besteiro

2016

Sci Rep

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Microtubule-based cytoskeletal structures have fundamental roles in several essential eukaryotic processes, including transport of intracellular constituents as well as ciliary and flagellar mobility. Temporal and spatial organisation of microtubules is determined by microtubule organising centers and a number of appendages and accessory proteins. Members of the SSNA1/DIP13 family are coiled coil proteins that are known to localise to microtubular structures like centrosomes and flagella, but are otherwise poorly characterised. We have identified a homologue of SSNA1/DIP13 in the parasitic protist Toxoplasma gondii and found it localises to parasite-specific cytoskeletal structures: the conoid in the apical complex of mature and dividing cells, and the basal complex in elongating daughter cells during cell division. This protein is dispensable for parasite growth in vitro. However, quite remarkably, this coiled coil protein is able to self-associate into higher order structures both in vitro and in vivo, and its overexpression is impairing parasite division.

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Targeted proteomic dissection of Toxoplasma cytoskeleton sub‐compartments using MORN1

Cited by 50 publications

References 61 publications

TgDrpC, an atypical dynamin‐related protein in Toxoplasma gondii, is associated with vesicular transport factors and parasite division

TgDrpC, an atypical dynamin‐related protein in Toxoplasma gondii, is associated with vesicular transport factors and parasite division

Targeting Toxoplasma Tubules: Tubulin, Microtubules, and Associated Proteins in a Human Pathogen

An evolutionarily conserved SSNA1/DIP13 homologue is a component of both basal and apical complexes of Toxoplasma gondii

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