ArticleEukaryotic cell2012
Molecular characterization of Toxoplasma gondii formin 3, an actin nucleator dispensable for tachyzoite growth and motility.
Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- Plasmodium falciparum formins are essential for invasion and sexual stage development.Communications biology · 2023Article
- Emerging Mechanisms of Endocytosis inLife (Basel, Switzerland) · 2021Review
- P18 (SRS35/TgSAG4) Plays a Role in the Invasion and Virulence ofFrontiers in immunology · 2021Article
- A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites.Nature communications · 2019Article
- Three F-actin assembly centers regulate organelle inheritance, cell-cell communication and motility ineLife · 2019Article
- Characterization of Toxoplasma DegP, a rhoptry serine protease crucial for lethal infection in mice.PloS one · 2017Article
- The conserved apicomplexan Aurora kinase TgArk3 is involved in endodyogeny, duplication rate and parasite virulence.Cellular microbiology · 2016Article
- Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?Acta crystallographica. Section F, Structural biology communications · 2015Review
- Lipid kinases are essential for apicoplast homeostasis in Toxoplasma gondii.Cellular microbiology · 2015Article
- Genetic manipulation in Δku80 strains for functional genomic analysis of Toxoplasma gondii.Journal of visualized experiments : JoVE · 2013Article
- Targeted proteomic dissection of Toxoplasma cytoskeleton sub-compartments using MORN1.Cytoskeleton (Hoboken, N.J.) · 2012Article
- Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro.Biochemistry · 2012Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxoplasma gondii belongs to the phylum Apicomplexa, a group of obligate intracellular parasites that rely on gliding motility to enter host cells. Drugs interfering with the actin cytoskeleton block parasite motility, host cell invasion, and egress from infected cells. Myosin A, profilin, formin 1, formin 2, and actin-depolymerizing factor have all been implicated in parasite motility, yet little is known regarding the importance of actin polymerization and other myosins for the remaining steps of the parasite lytic cycle. Here we establish that T. gondii formin 3 (TgFRM3), a newly described formin homology 2 domain (FH2)-containing protein, binds to Toxoplasma actin and nucleates rabbit actin assembly in vitro. TgFRM3 expressed as a transgene exhibits a patchy localization at several distinct structures within the parasite. Disruption of the TgFRM3 gene by double homologous recombination in a ku80-ko strain reveals no vital function for tachyzoite propagation in vitro, which is consistent with its weak level of expression in this life stage. Conditional stabilization of truncated forms of TgFRM3 suggests that different regions of the molecule contribute to distinct localizations. Moreover, expression of TgFRM3 lacking the C-terminal domain severely affects parasite growth and replication. This work provides a first insight into how this specialized formin, restricted to the group of coccidia, completes its actin-nucleating activity.
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