ArticleThe Journal of biological chemistry2010
Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 71 citations in OpenAlex.
- The cytoskeleton of pathogenic protists.Bioscience reports · 2026Review
- Serum Proteomic Changes in Pet Rabbits with Subclinical and Clinical Encephalitozoonosis in Thailand.Animals : an open access journal from MDPI · 2025Article
- Ubiquitin-activating enzyme1 (TgUAE1) acts as a key regulator of Toxoplasma gondii lytic cycle and homeostasis.Communications biology · 2025Article
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Functional characterization of CpADF, an actin depolymerizing factor protein in Cryptosporidium parvum.Parasitology research · 2023Article
- Mining the Proteome ofAnimals : an open access journal from MDPI · 2022Review
- Recombinant actin-depolymerizing factor of the apicomplexanFrontiers in cellular and infection microbiology · 2022Article
- Dominique Soldati-Favre: BringingFrontiers in cellular and infection microbiology · 2022Article
- Comparative and functional genomics of the protozoan parasite Babesia divergens highlighting the invasion and egress processes.PLoS neglected tropical diseases · 2019Article
- Three F-actin assembly centers regulate organelle inheritance, cell-cell communication and motility ineLife · 2019Article
- Gliding motility powers invasion and egress in Apicomplexa.Nature reviews. Microbiology · 2017Review
- The Molecular Basis of Erythrocyte Invasion by Malaria Parasites.Cell host & microbe · 2017Review
- Intranasal immunization with recombinant Toxoplasma gondii actin depolymerizing factor confers protective efficacy against toxoplasmosis in mice.BMC immunology · 2016Article
- Disassembly activity of actin-depolymerizing factor (ADF) is associated with distinct cellular processes in apicomplexan parasites.Molecular biology of the cell · 2015Article
- 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
- Solution structures and dynamics of ADF/cofilins UNC-60A and UNC-60B from Caenorhabditis elegans.The Biochemical journal · 2015Article
- Host cell invasion by apicomplexan parasites: the junction conundrum.PLoS pathogens · 2014Review
- A mechanism for actin filament severing by malaria parasite actin depolymerizing factor 1 via a low affinity binding interface.The Journal of biological chemistry · 2014Article
- Synthetic chondramide A analogues stabilize filamentous actin and block invasion by Toxoplasma gondii.Journal of natural products · 2013Article
- ATP-dependent regulation of actin monomer-filament equilibrium by cyclase-associated protein and ADF/cofilin.The Biochemical journal · 2013Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Toxoplasma gondii is a protozoan parasite belonging to the phylum Apicomplexa. Parasites in this phylum utilize a unique process of motility termed gliding, which is dependent on parasite actin filaments. Surprisingly, 98% of parasite actin is maintained as G-actin, suggesting that filaments are rapidly assembled and turned over. Little is known about the regulated disassembly of filaments in the Apicomplexa. In higher eukaryotes, the related actin depolymerizing factor (ADF) and cofilin proteins are essential regulators of actin filament turnover. ADF is one of the few actin-binding proteins conserved in apicomplexan parasites. In this study we examined the mechanism by which T. gondii ADF (TgADF) regulates actin filament turnover. Unlike other members of the ADF/cofilin (AC) family, apicomplexan ADFs lack key F-actin binding sites. Surprisingly, this promotes their enhanced disassembly of actin filaments. Restoration of the C-terminal F-actin binding site to TgADF stabilized its interaction with filaments but reduced its net filament disassembly activity. Analysis of severing activity revealed that TgADF is a weak severing protein, requiring much higher concentrations than typical AC proteins. Investigation of TgADF interaction with T. gondii actin (TgACT) revealed that TgADF disassembled short TgACT oligomers. Kinetic and steady-state polymerization assays demonstrated that TgADF has strong monomer-sequestering activity, inhibiting TgACT polymerization at very low concentrations. Collectively these data indicate that TgADF promoted the efficient turnover of actin filaments via weak severing of filaments and strong sequestering of monomers. This suggests a dual role for TgADF in maintaining high G-actin concentrations and effecting rapid filament turnover.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.