ArticleThe Journal of biological chemistry2012
Regulation of the Plasmodium motor complex: phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Complementary crosstalk between palmitoylation and phosphorylation events in MTIP regulates its role duringFrontiers in cellular and infection microbiology · 2022Article
- Structural role of essential light chains in the apicomplexan glideosome.Communications biology · 2020Article
- Full-lengtheLife · 2020Article
- Peptide Probes forACS chemical biology · 2020Article
- HOPPI-NMR: Hot-Peptide-Based Screening Assay for Inhibitors of Protein-Protein Interactions by NMR.ACS medicinal chemistry letters · 2020Article
- In vitro interaction between Plasmodium falciparum myosin B (PfMyoB) and myosin A tail interacting protein (MTIP).Parasitology research · 2018Article
- Dissecting the molecular assembly of 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
- 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.The Journal of biological chemistry · 2015Article
- Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?Acta crystallographica. Section F, Structural biology communications · 2015Review
- The apicomplexan glideosome and adhesins - Structures and function.Journal of structural biology · 2015Review
- Mutations in the P-type cation-transporter ATPase 4, PfATP4, mediate resistance to both aminopyrazole and spiroindolone antimalarials.ACS chemical biology · 2015Article
- Targeting a dynamic protein-protein interaction: fragment screening against the malaria myosin A motor complex.ChemMedChem · 2015Article
- A Toxoplasma gondii class XIV myosin, expressed in Sf9 cells with a parasite co-chaperone, requires two light chains for fast motility.The Journal of biological chemistry · 2014Article
- Unique apicomplexan IMC sub-compartment proteins are early markers for apical polarity in the malaria parasite.Biology open · 2013Article
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Authors and funding
9 authors.
Funding
Abstract
The interaction between the C-terminal tail of myosin A (MyoA) and its light chain, myosin A tail domain interacting protein (MTIP), is an essential feature of the conserved molecular machinery required for gliding motility and cell invasion by apicomplexan parasites. Recent data indicate that MTIP Ser-107 and/or Ser-108 are targeted for intracellular phosphorylation. Using an optimized MyoA tail peptide to reconstitute the complex, we show that this region of MTIP is an interaction hotspot using x-ray crystallography and NMR, and S107E and S108E mutants were generated to mimic the effect of phosphorylation. NMR relaxation experiments and other biophysical measurements indicate that the S108E mutation serves to break the tight clamp around the MyoA tail, whereas S107E has a smaller but measurable impact. These data are consistent with physical interactions observed between recombinant MTIP and native MyoA from Plasmodium falciparum lysates. Taken together these data support the notion that the conserved interactions between MTIP and MyoA may be specifically modulated by this post-translational modification.
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