title: Plasmodium motility: actin not actin' like actin.
abstract: Apicomplexan parasites such as Plasmodium and Toxoplasma display actomyosin-dependent motility in the absence of readily detectable actin polymers. Three recent studies indicate that parasite actin polymers, either harvested from parasites or formed from purified recombinant proteins, are exceptionally short ( approximately 100 nm). We propose that parasite motility could be directed by the transient formation of short actin filament scaffolds. Parasite actin polymers that support transmembrane receptors are pulled, by myosin interaction, backwards along the parasite periphery, resulting in forward movement.
authors.affiliation: Max Delbrück Center for Molecular Medicine, 13125 Berlin, Germany. schueler@mdc-berlin.de
authors.forename: Herwig
authors.initials: H
authors.lastname: Schüler
authors.forename: Kai
authors.initials: K
authors.lastname: Matuschewski
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry / Q000502:physiology*; D000199:Actins / Q000737:chemistry / Q000502:physiology*; D000205:Actomyosin / Q000502:physiology; D000818:Animals; D009068:Movement / Q000502:physiology; D010961:Plasmodium / Q000737:chemistry / Q000502:physiology*
chemical_list: D000199:Actins; D000205:Actomyosin