ArticleThe Journal of biological chemistry2015
The Plasmodium Class XIV Myosin, MyoB, Has a Distinct Subcellular Location in Invasive and Motile Stages of the Malaria Parasite and an Unusual Light Chain.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
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- Article
- Plasmodium falciparum PfMyoF contains a Rab-like tail domain and associates with perinuclear membrane trafficking proteins.Communications biology · 2026Article
- Integrative genomics ofbioRxiv : the preprint server for biology · 2026Article
- A subpellicular microtubule dynein transport machinery regulates ookinete morphogenesis for mosquito transmission of Plasmodium yoelii.Nature communications · 2024Article
- Apical anchorage and stabilization of subpellicular microtubules by apical polar ring ensures Plasmodium ookinete infection in mosquito.Nature communications · 2022Article
- Expansion microscopy provides new insights into the cytoskeleton of malaria parasites including the conservation of a conoid.PLoS biology · 2021Article
- Actomyosin forces and the energetics of red blood cell invasion by the malaria parasite Plasmodium falciparum.PLoS pathogens · 2020Article
- The Myosin Family of Mechanoenzymes: From Mechanisms to Therapeutic Approaches.Annual review of biochemistry · 2020Review
- Systematic analysis of Plasmodium myosins reveals differential expression, localisation, and function in invasive and proliferative parasite stages.Cellular microbiology · 2019Article
- Divergent roles for the RH5 complex components, CyRPA and RIPR in human-infective malaria parasites.PLoS pathogens · 2019Article
- Proteins with calmodulin-like domains: structures and functional roles.Cellular and molecular life sciences : CMLS · 2019Review
- In vitro interaction between Plasmodium falciparum myosin B (PfMyoB) and myosin A tail interacting protein (MTIP).Parasitology research · 2018Article
- Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development.Scientific reports · 2017Article
- Gliding motility powers invasion and egress in Apicomplexa.Nature reviews. Microbiology · 2017Review
- Compositional and expression analyses of the glideosome during theThe Journal of biological chemistry · 2017Article
- Myosin B of Plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP.Parasitology research · 2017Article
- The Binding of Plasmodium falciparum Adhesins and Erythrocyte Invasion Proteins to Aldolase Is Enhanced by Phosphorylation.PloS one · 2016Article
- Revisiting Myosin Families Through Large-scale Sequence Searches Leads to the Discovery of New Myosins.Evolutionary bioinformatics online · 2016Article
- The Conoid Associated Motor MyoH Is Indispensable for Toxoplasma gondii Entry and Exit from Host Cells.PLoS pathogens · 2016Article
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Authors and funding
14 authors at 3 institutions in 3 countries.
Funding
Abstract
Myosin B (MyoB) is one of the two short class XIV myosins encoded in the Plasmodium genome. Class XIV myosins are characterized by a catalytic "head," a modified "neck," and the absence of a "tail" region. Myosin A (MyoA), the other class XIV myosin in Plasmodium, has been established as a component of the glideosome complex important in motility and cell invasion, but MyoB is not well characterized. We analyzed the properties of MyoB using three parasite species as follows: Plasmodium falciparum, Plasmodium berghei, and Plasmodium knowlesi. MyoB is expressed in all invasive stages (merozoites, ookinetes, and sporozoites) of the life cycle, and the protein is found in a discrete apical location in these polarized cells. In P. falciparum, MyoB is synthesized very late in schizogony/merogony, and its location in merozoites is distinct from, and anterior to, that of a range of known proteins present in the rhoptries, rhoptry neck or micronemes. Unlike MyoA, MyoB is not associated with glideosome complex proteins, including the MyoA light chain, myosin A tail domain-interacting protein (MTIP). A unique MyoB light chain (MLC-B) was identified that contains a calmodulin-like domain at the C terminus and an extended N-terminal region. MLC-B localizes to the same extreme apical pole in the cell as MyoB, and the two proteins form a complex. We propose that MLC-B is a MyoB-specific light chain, and for the short class XIV myosins that lack a tail region, the atypical myosin light chains may fulfill that role.
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