An Apicomplexan Actin-Binding Protein Serves as a Connector and Lipid Sensor to Coordinate Motility and Invasion
| العنوان: | An Apicomplexan Actin-Binding Protein Serves as a Connector and Lipid Sensor to Coordinate Motility and Invasion |
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| المؤلفون: | Inari Kursula, Nicolò Tosetti, Huijong Han, Jessica Stock, Damien Jacot, Dominique Soldati-Favre, Yu-Fu Hung, Rita Tewari, Arnault Graindorge, Isa Pires |
| المصدر: | Cell Host & Microbe, Vol. 20, No 6 (2016) pp. 731-743 |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0301 basic medicine, Models, Molecular, Gliding motility, Plasmodium berghei, Protein Conformation, 030106 microbiology, Protozoan Proteins, Motility, Phosphatidic Acids, Microbiology, Filamentous actin, Exocytosis, Microneme, 03 medical and health sciences, Cell Movement, Virology, parasitic diseases, Animals, Actin-binding protein, ddc:616, Organelles, Protozoan Infections, biology, Molecular Motor Proteins, Microfilament Proteins, Membrane Proteins, Methyltransferases, Lipids, Transmembrane protein, Actins, 3. Good health, Cell biology, Pleckstrin homology domain, Actin Cytoskeleton, 030104 developmental biology, biology.protein, Parasitology, Rabbits, Apicomplexa, Cell Adhesion Molecules, Toxoplasma, Toxoplasmosis |
| الوصف: | Apicomplexa exhibit a unique form of substrate-dependent gliding motility central for host cell invasion and parasite dissemination. Gliding is powered by rearward translocation of apically secreted transmembrane adhesins via their interaction with the parasite actomyosin system. We report a conserved armadillo and pleckstrin homology (PH) domain-containing protein, termed glideosome-associated connector (GAC), that mediates apicomplexan gliding motility, invasion, and egress by connecting the micronemal adhesins with the actomyosin system. TgGAC binds to and stabilizes filamentous actin and specifically associates with the transmembrane adhesin TgMIC2. GAC localizes to the apical pole in invasive stages of Toxoplasma gondii and Plasmodium berghei, and apical positioning of TgGAC depends on an apical lysine methyltransferase, TgAKMT. GAC PH domain also binds to phosphatidic acid, a lipid mediator associated with microneme exocytosis. Collectively, these findings indicate a central role for GAC in spatially and temporally coordinating gliding motility and invasion. |
| تدمد: | 1934-6069 1931-3128 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::600c6add85469b36643d0d2286f3b751 https://pubmed.ncbi.nlm.nih.gov/27978434 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....600c6add85469b36643d0d2286f3b751 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19346069 19313128 |
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