Functional dissection of the apicomplexan glideosome molecular architecture
| Autor: | Valérie Polonais, Julien Limenitakis, Karine Frénal, Rolf Stratmann, Jean-Baptiste Marq, Dominique Soldati-Favre |
|---|---|
| Přispěvatelé: | Département de Microbiologie et Médecine moléculaire, Université de Genève (UNIGE), Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Centre National de la Recherche Scientifique (CNRS), Projekttrager Julich & Projekttrager Deutsch Zent, D-53227 Bonn, Germany, Université de Genève = University of Geneva (UNIGE) |
| Rok vydání: | 2010 |
| Předmět: |
Cancer Research
Acylation Protozoan Proteins MESH: Amino Acid Sequence Conserved sequence Cell membrane Myosin MESH: Protozoan Proteins Peptide sequence MESH: Plasmodium falciparum Cells Cultured Conserved Sequence ddc:616 MESH: Genetic Complementation Test 0303 health sciences MESH: Conserved Sequence MESH: Toxoplasma 030302 biochemistry & molecular biology MESH: Myosin Light Chains Cell biology medicine.anatomical_structure MESH: Membrane Proteins Toxoplasma MESH: Cells Cultured Myosin light-chain kinase Myosin Light Chains Molecular Sequence Data Plasmodium falciparum Biology MESH: Actins Transfection MESH: Host-Parasite Interactions Microbiology Host-Parasite Interactions 03 medical and health sciences Virology Immunology and Microbiology(all) parasitic diseases medicine Humans [SDV.MP.PAR]Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology Amino Acid Sequence Molecular Biology Actin 030304 developmental biology MESH: Acylation Inner membrane complex MESH: Molecular Sequence Data MESH: Humans MESH: Transfection Cell Membrane Genetic Complementation Test Membrane Proteins Actins Membrane protein Parasitology MESH: Cell Membrane |
| Zdroj: | Cell host & microbe, Vol. 8, No 4 (2010) pp. 343-57 Cell Host and Microbe Cell Host and Microbe, Elsevier, 2010, 8 (4), pp.343-57. ⟨10.1016/j.chom.2010.09.002⟩ Cell Host & Microbe; Vol 8 Cell Host and Microbe, 2010, 8 (4), pp.343-57. ⟨10.1016/j.chom.2010.09.002⟩ |
| ISSN: | 1934-6069 1931-3128 |
| DOI: | 10.1016/j.chom.2010.09.002⟩ |
| Popis: | International audience; The glideosome of apicomplexan parasites is an actin- and myosin-based machine located at the pellicle, between the plasma membrane (PM) and inner membrane complex (IMC), that powers parasite motility, migration, and host cell invasion and egress. It is composed of myosin A, its light chain MLC1, and two gliding-associated proteins, GAP50 and GAP45. We identify GAP40, a polytopic protein of the IMC, as an additional glideosome component and show that GAP45 is anchored to the PM and IMC via its N- and C-terminal extremities, respectively. While the C-terminal region of GAP45 recruits MLC1-MyoA to the IMC, the N-terminal acylation and coiled-coil domain preserve pellicle integrity during invasion. GAP45 is essential for gliding, invasion, and egress. The orthologous Plasmodium falciparum GAP45 can fulfill this dual function, as shown by transgenera complementation, whereas the coccidian GAP45 homolog (designated here as) GAP70 specifically recruits the glideosome to the apical cap of the parasite. |
| Databáze: | OpenAIRE |
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