ArticleThe Biochemical journal2007
The toxofilin-actin-PP2C complex of Toxoplasma: identification of interacting domains.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Mapping amBio · 2025Article
- The plant-like protein phosphatase PPKL regulates parasite replication and morphology in Toxoplasma gondii.Parasites & vectors · 2024Article
- Deciphering the Role of Protein Phosphatases in Apicomplexa: The Future of Innovative Therapeutics?Microorganisms · 2022Review
- The serine/threonine phosphatases of apicomplexan parasites.Molecular microbiology · 2017Review
- The Toxoplasma gondii inhibitor-2 regulates protein phosphatase 1 activity through multiple motifs.Parasitology research · 2017Article
- Dopamine D2 receptor relies upon PPM/PP2C protein phosphatases to dephosphorylate huntingtin protein.The Journal of biological chemistry · 2014Article
- Identification of differentially expressed proteins in sulfadiazine resistant and sensitive strains of Toxoplasma gondii using difference-gel electrophoresis (DIGE).International journal for parasitology. Drugs and drug resistance · 2013Article
- Specific targeting of caspase-9/PP2A interaction as potential new anti-cancer therapy.PloS one · 2013Article
- Toxofilin upregulates the host cortical actin cytoskeleton dynamics, facilitating Toxoplasma invasion.Journal of cell science · 2012Article
- GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex.Eukaryotic cell · 2009Article
- IDENTIFICATION OF CONOIDIN A AS A COVALENT INHIBITOR OF PEROXIREDOXIN II.Organic & biomolecular chemistry · 2009Article
- Toxofilin from Toxoplasma gondii forms a ternary complex with an antiparallel actin dimer.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- A Toxoplasma gondii leucine-rich repeat protein binds phosphatase type 1 protein and negatively regulates its activity.Eukaryotic cell · 2007Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxofilin is a 27 kDa protein isolated from the human protozoan parasite Toxoplasma gondii, which causes toxoplasmosis. Toxofilin binds to G-actin, and in vitro studies have shown that it controls elongation of actin filaments by sequestering actin monomers. Toxofilin affinity for G-actin is controlled by the phosphorylation status of its Ser53, which depends on the activities of a casein kinase II and a type 2C serine/threonine phosphatase (PP2C). To get insights into the functional properties of toxofilin, we undertook a structure-function analysis of the protein using a combination of biochemical techniques. We identified a domain that was sufficient to sequester G-actin and that contains three peptide sequences selectively binding to G-actin. Two of these sequences are similar to sequences present in several G- and F-actin-binding proteins, while the third appears to be specific to toxofilin. Additionally, we identified two toxofilin domains that interact with PP2C, one of which contains the Ser53 substrate. In addition to characterizing the interacting domains of toxofilin with its partners, the present study also provides information on an in vivo-based approach to selectively and competitively disrupt the protein-protein interactions that are important to parasite motility.
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