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Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites
Journal article   Open access   Peer reviewed

Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites

Lawrence W Bergman, Karine Kaiser, Hisashi Fujioka, Isabelle Coppens, Thomas M Daly, Sarah Fox, Kai Matuschewski, Victor Nussenzweig and Stefan H I Kappe
Journal of cell science, v 116(Pt 1), pp 39-49
01 Jan 2003
DOI: https://doi.org/10.1242/jcs.00194
PMID: 12456714
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://doi.org/10.1242/jcs.00194View
Published, Version of Record (VoR) Open

Abstract

Cytoskeletal Proteins Protein Binding - genetics Humans DNA, Complementary - genetics Plasmodium yoelii - ultrastructure Molecular Sequence Data Amino Acid Sequence - genetics Protozoan Proteins - genetics Molecular Motor Proteins - genetics Plasmodium yoelii - metabolism Cell Movement - genetics Nonmuscle Myosin Type IIA - metabolism Host-Parasite Interactions - genetics Protozoan Proteins - metabolism Cell Membrane - metabolism Tumor Cells, Cultured Actin Cytoskeleton - genetics Sporozoites - pathogenicity DNA, Complementary - analysis Base Sequence - genetics Membrane Proteins - isolation & purification Actin Cytoskeleton - metabolism Membrane Proteins - genetics Cell Compartmentation - genetics Cell Membrane - ultrastructure Protein Structure, Tertiary - genetics Microscopy, Electron Sporozoites - ultrastructure Macromolecular Substances Carrier Proteins - genetics Two-Hybrid System Techniques Plasmodium yoelii - pathogenicity Animals Models, Biological Molecular Motor Proteins - isolation & purification Carrier Proteins - isolation & purification Sporozoites - metabolism
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.

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Collaboration types
Domestic collaboration
Web of Science research areas
Cell Biology
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