Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex ofPlasmodiumsporozoites
| Autor: | Sarah Fox, Stefan H. I. Kappe, Victor Nussenzweig, Thomas M. Daly, Lawrence W. Bergman, Isabelle Coppens, Hisashi Fujioka, Kai Matuschewski, Karine Kaiser |
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| Rok vydání: | 2003 |
| Předmět: |
DNA
Complementary Macromolecular Substances Gliding motility Molecular Sequence Data Protozoan Proteins Biology Models Biological Host-Parasite Interactions Motor protein Protein structure Cell Movement Two-Hybrid System Techniques Myosin Tumor Cells Cultured Animals Humans Amino Acid Sequence Cytoskeleton Actin Inner membrane complex Base Sequence Molecular Motor Proteins Nonmuscle Myosin Type IIA Cell Membrane Membrane Proteins Plasmodium yoelii Cell Biology Transmembrane protein Cell Compartmentation Protein Structure Tertiary Cell biology Actin Cytoskeleton Cytoskeletal Proteins Microscopy Electron Sporozoites Carrier Proteins Protein Binding |
| Zdroj: | Journal of Cell Science. 116:39-49 |
| ISSN: | 1477-9137 0021-9533 |
| DOI: | 10.1242/jcs.00194 |
| Popis: | Apicomplexan host cell invasion and gliding motility depend on the parasite's actomyosin system located beneath the plasma membrane of invasive stages. Myosin A (MyoA), a class XIV unconventional myosin, is the motor protein. A model has been proposed to explain how the actomyosin motor operates but little is known about the components, topology and connectivity of the motor complex. Using the MyoA neck and tail domain as bait in a yeast two-hybrid screen we identified MTIP, a novel 24 kDa protein that interacts with MyoA. Deletion analysis shows that the 15 amino-acid C-terminal tail domain of MyoA, rather than the neck domain, specifically interacts with MTIP. In Plasmodium sporozoites MTIP localizes to the inner membrane complex (IMC), where it is found clustered with MyoA. The data support a model for apicomplexan motility and invasion in which the MyoA motor protein is associated via its tail domain with MTIP, immobilizing it at the outer IMC membrane. The head domain of the immobilized MyoA moves actin filaments that,directly or via a bridging protein, connect to the cytoplasmic domain of a transmembrane protein of the TRAP family. The actin/TRAP complex is then redistributed by the stationary MyoA from the anterior to the posterior end of the zoite, leading to its forward movement on a substrate or to penetration of a host cell. |
| Databáze: | OpenAIRE |
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