ArticlePLoS pathogens2014
Plasticity between MyoC- and MyoA-glideosomes: an example of functional compensation in Toxoplasma gondii invasion.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 106 citations in OpenAlex.
- Identification and characterization of factors that govern apicoplast segregation in Toxoplasma gondii.Nature communications · 2026Article
- Toxoplasma IMC1 is a central component of the subpellicular network and plays critical roles in parasite morphology, replication, and infectivity.PLoS pathogens · 2026Article
- Bumped Kinase Inhibitor BKI-1708 Interferes in Cytokinesis and Drives Baryzoite Conversion in the Cyst-Forming Apicomplexan ParasitesInternational journal of molecular sciences · 2026Article
- Two anchoring proteins control daughter apical complex assembly inbioRxiv : the preprint server for biology · 2026Article
- Function and interactions of a protein bridge between the inner membrane complex and subpellicular microtubules inMolecular biology of the cell · 2025Article
- Phosphatase UBLCP1 is required for the growth, virulence and mitochondrial integrity of Toxoplasma gondii.Parasites & vectors · 2025Article
- Characterization and functional analysis ofmBio · 2024Article
- Myosin A and F-Actin play a critical role in mitochondrial dynamics and inheritance in Toxoplasma gondii.PLoS pathogens · 2024Article
- Alveolin proteins in the Toxoplasma inner membrane complex form a highly interconnected structure that maintains parasite shape and replication.PLoS biology · 2024Article
- Cytokinetic abscission in Toxoplasma gondii is governed by protein phosphatase 2A and the daughter cell scaffold complex.The EMBO journal · 2024Article
- PP1 phosphatase controls both daughter cell formation and amylopectin levels in Toxoplasma gondii.PLoS biology · 2024Article
- Systematic characterization of all Toxoplasma gondii TBC domain-containing proteins identifies an essential regulator of Rab2 in the secretory pathway.PLoS biology · 2024Article
- Myosin A and F-Actin play a critical role in mitochondrial dynamics and inheritance inbioRxiv : the preprint server for biology · 2024Article
- MyosinA is a druggable target in the widespread protozoan parasite Toxoplasma gondii.PLoS biology · 2023Article
- IMC29 Plays an Important Role inmBio · 2023Article
- An apical membrane complex for triggering rhoptry exocytosis and invasion in Toxoplasma.The EMBO journal · 2022Article
- Conoid extrusion regulates glideosome assembly to control motility and invasion in Apicomplexa.Nature microbiology · 2022Article
- Temporal and thermal profiling of theeLife · 2022Article
- Marine gregarine genomes reveal the breadth of apicomplexan diversity with a partially conserved glideosome machinery.BMC genomics · 2022Article
- Identification of new components of the basal pole ofFrontiers in cellular and infection microbiology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The glideosome is an actomyosin-based machinery that powers motility in Apicomplexa and participates in host cell invasion and egress from infected cells. The central component of the glideosome, myosin A (MyoA), is a motor recruited at the pellicle by the acylated gliding-associated protein GAP45. In Toxoplasma gondii, GAP45 also contributes to the cohesion of the pellicle, composed of the inner membrane complex (IMC) and the plasma membrane, during motor traction. GAP70 was previously identified as a paralog of GAP45 that is tailored to recruit MyoA at the apical cap in the coccidian subgroup of the Apicomplexa. A third member of this family, GAP80, is demonstrated here to assemble a new glideosome, which recruits the class XIV myosin C (MyoC) at the basal polar ring. MyoC shares the same myosin light chains as MyoA and also interacts with the integral IMC proteins GAP50 and GAP40. Moreover, a central component of this complex, the IMC-associated protein 1 (IAP1), acts as the key determinant for the restricted localization of MyoC to the posterior pole. Deletion of specific components of the MyoC-glideosome underscores the installation of compensatory mechanisms with components of the MyoA-glideosome. Conversely, removal of MyoA leads to the relocalization of MyoC along the pellicle and at the apical cap that accounts for residual invasion. The two glideosomes exhibit a considerable level of plasticity to ensure parasite survival.
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