ArticlePLoS pathogens2019
A unique dynamin-related protein is essential for mitochondrial fission in Toxoplasma gondii.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- The trypanosomatid dynamin-like protein associates with glycosomes.bioRxiv : the preprint server for biology · 2026Article
- The segregation of organelles and organellar genomes across eukaryotic biology.Biochemical Society transactions · 2026Review
- A Spinster-like Transporter at the Inner Membrane Complex is critical for Toxoplasma gondii cytokinesis, motility and invasion.PLoS pathogens · 2026Article
- Phosphatase UBLCP1 is required for the growth, virulence and mitochondrial integrity of Toxoplasma gondii.Parasites & vectors · 2025Article
- The dynamin-related protein PfDyn2 is essential for both apicoplast and mitochondrial fission inmBio · 2025Article
- Pathogen-induced mitochondrial dysfunction: mechanistic insights, immune crosstalk, and therapeutic opportunities.Frontiers in cellular and infection microbiology · 2025Review
- Timing of dense granule biogenesis in asexual malaria parasites.Microbiology (Reading, England) · 2023Article
- Stable endocytic structures navigate the complex pellicle of apicomplexan parasites.Nature communications · 2023Article
- The Toxoplasma micropore mediates endocytosis for selective nutrient salvage from host cell compartments.Nature communications · 2023Article
- IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion-pellicle contact sites in Toxoplasma gondii.Journal of cell science · 2022Article
- Temporal and thermal profiling of theeLife · 2022Article
- Article
- Comparative Phosphoproteomic Analysis of Sporulated Oocysts and Tachyzoites ofMolecules (Basel, Switzerland) · 2022Article
- Article
- Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum.Journal of cell science · 2021Article
- Review
- Dual RNA Sequencing Meta-analysis inmSystems · 2021Article
- Next-generation yeast-two-hybrid analysis with Y2H-SCORES identifies novel interactors of the MLA immune receptor.PLoS computational biology · 2021Article
- Review
- The Ringleaders: Understanding the Apicomplexan Basal Complex Through Comparison to Established Contractile Ring Systems.Frontiers in cellular and infection microbiology · 2021Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The single mitochondrion of apicomplexan protozoa is thought to be critical for all stages of the life cycle, and is a validated drug target against these important human and veterinary parasites. In contrast to other eukaryotes, replication of the mitochondrion is tightly linked to the cell cycle. A key step in mitochondrial segregation is the fission event, which in many eukaryotes occurs by the action of dynamins constricting the outer membrane of the mitochondria from the cytosolic face. To date, none of the components of the apicomplexan fission machinery have been identified and validated. We identify here a highly divergent, dynamin-related protein (TgDrpC), conserved in apicomplexans as essential for mitochondrial biogenesis and potentially for fission in Toxoplasma gondii. We show that TgDrpC is found adjacent to the mitochondrion, and is localised both at its periphery and at its basal part, where fission is expected to occur. We demonstrate that depletion or dominant negative expression of TgDrpC results in interconnected mitochondria and ultimately in drastic changes in mitochondrial morphology, as well as in parasite death. Intriguingly, we find that the canonical adaptor TgFis1 is not required for mitochondrial fission. The identification of an Apicomplexa-specific enzyme required for mitochondrial biogenesis and essential for parasite growth highlights parasite adaptation. This work paves the way for future drug development targeting TgDrpC, and for the analysis of additional partners involved in this crucial step of apicomplexan multiplication.
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