ArticleEukaryotic cell2013
Novel thioredoxin-like proteins are components of a protein complex coating the cortical microtubules of Toxoplasma gondii.
Article in Eukaryotic cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 70 citations in OpenAlex.
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- An apical ring protein essential for conoid complex assembly and daughter cell formation in Toxoplasma gondii.Nature communications · 2025Article
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- Function and interactions of a protein bridge between the inner membrane complex and subpellicular microtubules inMolecular biology of the cell · 2025Article
- Microtubule inner proteins ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The initiation and early development of apical-basal polarity in Toxoplasma gondii.Journal of cell science · 2024Article
- SPARK regulates AGC kinases central to theeLife · 2024Article
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- The initiation and early development of the tubulin-containing cytoskeleton in the human parasiteMolecular biology of the cell · 2024Article
- Sustained rhoptry docking and discharge requires Toxoplasma gondii intraconoidal microtubule-associated proteins.Nature communications · 2024Article
- The cortical microtubules of Toxoplasma gondii underlie the helicity of parasite movement.Journal of cell science · 2023Article
- The protein phosphatase PPKL is a key regulator of daughter parasite development inbioRxiv : the preprint server for biology · 2023Article
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- SPACA9 is a lumenal protein of human ciliary singlet and doublet microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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7 authors at 3 institutions in 2 countries.
Funding
Abstract
Microtubules are versatile biopolymers that support numerous vital cellular functions in eukaryotes. The specific properties of microtubules are dependent on distinct microtubule-associated proteins, as the tubulin subunits and microtubule structure are exceptionally conserved. Highly specialized microtubule-containing assemblies are often found in protists, which are rich sources for novel microtubule-associated proteins. A protozoan parasite, Toxoplasma gondii, possesses several distinct tubulin-containing structures, including 22 microtubules closely associated with the cortical membrane. Early ultrastructural studies have shown that the cortical microtubules are heavily decorated with associating proteins. However, little is known about the identities of these proteins. Here, we report the discovery of a novel protein, TrxL1 (for Thioredoxin-Like protein 1), and an associating complex that coats the cortical microtubules. TrxL1 contains a thioredoxin-like fold. To visualize its localization in live parasites by fluorescence, we replaced the endogenous TrxL1 gene with an mEmeraldFP-TrxL1 fusion gene. Structured illumination-based superresolution imaging of this parasite line produced a detailed view of the microtubule cytoskeleton. Despite its stable association with the cortical microtubules in the parasite, TrxL1 does not seem to bind to microtubules directly. Coimmunoprecipitation experiments showed that TrxL1 associates with a protein complex containing SPM1, a previously reported microtubule-associated protein in T. gondii. We also found that SPM1 recruits TrxL1 to the cortical microtubules. Besides SPM1, several other novel proteins are found in the TrxL1-containing complex, including TrxL2, a close homolog of TrxL1. Thus, our results reveal for the first time a microtubule-associated complex in T. gondii.
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