Affinage · Toxoplasma gondii

MyoA

myosin A · UniProt S8G527

Annotated
2026-09-10
29 papers in source corpus 23 papers cited in narrative 23 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

Toxoplasma gondii MyoA is a fast, single-headed, plus-end-directed unconventional myosin that forms the mechanochemical core of the glideosome, the pellicular actomyosin motor powering parasite gliding, host-cell invasion, egress, and mitochondrial inheritance (PMID:11980712, PMID:12399593, PMID:39374269). As purified motor it moves actin filaments in 5.3-nm unitary steps at ~5.2 µm/s and binds the novel light chain MLC1 while anchored at the plasma membrane (PMID:11980712). Within the parasite the motor assembles into a complex of MLC1, GAP45, and the integral IMC glycoprotein GAP50, which anchors the motor to the inner membrane complex through a spatially controlled, staged assembly process (PMID:15123738, PMID:20951968); final docking onto GAP50 is gated by GAP45 phosphorylation at Ser163/Ser167 (PMID:19047362). Fast motility requires two light chains on the MyoA lever arm: MLC1 clamps the neck with nanomolar affinity and cooperatively promotes high-affinity binding of an essential light chain (ELC1/ELC2), whose engagement of the neck and converter subdomain stiffens the lever arm and raises gliding speed (PMID:25231988, PMID:28972141, PMID:33051581, PMID:26374117). Motor output is tuned by calcium-dependent phosphorylation — TgCDPK3 phosphorylates MyoA at Ser21 and Ser743 to enable rapid initiation of motility and egress (PMID:24989796, PMID:26544049) — and by post-translational modification of MLC1, including covalent modification at Cys58 by the inhibitor tachyplegin (PMID:20084115, PMID:24892871). MyoA is essential for pathogenesis and invasion in vivo, though conditional loss is partially compensated by relocalization of MyoC glideosomes (PMID:12399593, PMID:25393004); the actomyosin system functions particularly in substrate attachment and traction-force generation during helical gliding (PMID:28100223, PMID:32432851). Crystallographic and HDX-MS studies define a divergent motor-domain architecture with a class-defining SH1/SH2 region and drug-accessible pockets distinct from human myosins, validating MyoA as a parasite-specific small-molecule target as demonstrated by the ATPase inhibitor KNX-002 (PMID:30348763, PMID:37155705).

Mechanistic history

Synthesis pass · year-by-year structured walk · 23 steps
  1. 2001 Medium

    Before its motor properties were known, MyoA was shown to be under tight protein-level feedback control, establishing that its abundance is homeostatically regulated.

    Evidence Tetracycline-inducible overexpression with Western blot of endogenous protein

    PMID:11713335

    Open questions at the time
    • Mechanism of feedback down-regulation unresolved
    • No link to motor function established at this stage
  2. 2002 High

    The question of what kind of motor MyoA is was answered by direct biophysical reconstitution, defining it as a fast, single-headed, plus-end-directed myosin bound to a novel light chain MLC1 and localized at the plasma membrane.

    Evidence In vitro motility assay, optical-trap single-molecule measurement of purified motor complex

    PMID:11980712

    Open questions at the time
    • Full light-chain complement not yet defined
    • Membrane anchoring proteins not yet identified
  3. 2002 High

    Whether the motor mattered for the parasite lifecycle was settled by conditional disruption, showing MyoA is essential for host-cell invasion, spreading, and pathogenesis in vivo.

    Evidence Tetracycline-inducible conditional gene disruption, invasion assays, animal infection model

    PMID:12399593

    Open questions at the time
    • Molecular basis of the invasion defect not dissected
    • Did not address whether other myosins compensate
  4. 2004 High

    The architecture anchoring the motor to the parasite was defined by identifying the MyoA-MLC1-GAP45-GAP50 complex on the inner membrane complex, with GAP50 as the integral-membrane anchor and assembly occurring in stages.

    Evidence Reciprocal co-immunoprecipitation, subcellular fractionation, immunofluorescence

    PMID:15123738

    Open questions at the time
    • Trigger controlling staged assembly unknown
    • Force transduction from motor to membrane not measured
  5. 2008 High

    How the final assembly step is regulated was answered by showing GAP45 phosphorylation at Ser163/Ser167 controls docking of the MyoA-MLC1-GAP45 subcomplex onto the GAP50 anchor.

    Evidence Mass spectrometry site identification, phosphomimetic/alanine mutagenesis, co-immunoprecipitation

    PMID:19047362

    Open questions at the time
    • Kinase responsible for these sites not identified
    • Temporal coupling to invasion not shown
  6. 2010 High

    The glideosome roster and membrane tethering were extended by identifying GAP40 and mapping GAP45 as the bridge that recruits MLC1-MyoA from plasma membrane to IMC, essential for gliding, invasion, and egress.

    Evidence Conditional knockdown, co-IP, immunofluorescence, cross-species complementation with P. falciparum GAP45

    PMID:20951968

    Open questions at the time
    • GAP40 molecular role undefined
    • Quantitative contribution of tethering to force output unknown
  7. 2010 High

    That motor activity can be chemically modulated through its light chain was shown when tachyplegin-induced modification of MLC1 reduced MyoA motility in vitro.

    Evidence In vitro motility assay of motor complexes from treated vs untreated parasites, mobility shift, peptide mapping

    PMID:20084115

    Open questions at the time
    • Precise chemical adduct on MLC1 not yet localized
    • Mechanism linking MLC1 modification to motor slowing unresolved
  8. 2011 Medium

    Calcium signaling was tied to motor regulation by showing calcium-dependent phosphorylation across GAP45, MLC1, and MyoA and calcium-enhanced recruitment of a new essential light chain (ELC).

    Evidence SILAC quantitative phosphoproteomics, 2-DE of 32P-labeled extracts, calcium stimulation

    PMID:21980283

    Open questions at the time
    • Causal link between phosphorylation and activity correlative only
    • Responsible kinase(s) not identified
  9. 2014 High

    The two-light-chain requirement for fast motility was reconstituted heterologously, showing MyoA needs the UCS co-chaperone TgUNC for folding and that ELC1 addition to MLC1 more than doubles gliding speed.

    Evidence Baculovirus/Sf9 expression with co-chaperone and light-chain co-expression, in vitro actin gliding assays

    PMID:25231988

    Open questions at the time
    • In-cell requirement for TgUNC not demonstrated
    • Structural basis of speed enhancement not resolved here
  10. 2014 Medium

    The apparent absolute essentiality of MyoA was revised by conditional KO showing residual invasion, implying alternative invasion mechanisms.

    Evidence Conditional knockout of MyoA/MLC1/GAP45/Act1, invasion and motility assays

    PMID:24632839

    Open questions at the time
    • Nature of the alternative mechanism not defined in this study
    • Extent of compensation across strains unaddressed
  11. 2014 Medium

    The source of residual invasion was traced to glideosome plasticity, with MyoC relocalizing along the pellicle and apical cap to compensate for MyoA loss.

    Evidence Conditional MyoA knockout, MyoC immunofluorescence localization, invasion assays

    PMID:25393004

    Open questions at the time
    • Trigger for MyoC redistribution unknown
    • Whether MyoC fully substitutes for MyoA force output not quantified
  12. 2014 High

    Direct functional proof that calcium-dependent MyoA phosphorylation modulates motility came from nonphosphorylatable mutants egressing more slowly under calcium ionophore.

    Evidence Site-directed mutagenesis of phosphosites, calcium ionophore treatment, egress assays, calcium measurement

    PMID:24989796

    Open questions at the time
    • Kinase not identified in this study
    • Individual phosphosite contributions not separated
  13. 2014 High

    The covalent target of tachyplegin was pinned to MLC1 Cys58, establishing the mechanistic route by which the compound inhibits MyoA motor activity.

    Evidence Click chemistry labelling, C58S/S57A mutagenesis, knock-in parasites, 3D motility assay

    PMID:24892871

    Open questions at the time
    • How Cys58 modification propagates to the motor domain not structurally defined
  14. 2015 High

    The writer of MyoA regulatory phosphorylation was identified as TgCDPK3 acting at Ser21 and Ser743, with separation-of-function mutants tying these sites to rapid motility initiation and egress.

    Evidence BioID screen, in vitro peptide-array kinase assay, complementation with phosphomimetic/alanine mutants, egress assays

    PMID:26544049

    Open questions at the time
    • Structural consequence of phosphorylation on motor cycle not directly shown here
    • Whether other kinases contribute in vivo unresolved
  15. 2015 Medium

    The essential light chains ELC1 and ELC2 were shown to be redundant lever-arm components whose calcium-promoted contacts with MLC1 stabilize the lever arm and support invasion, egress, and motility.

    Evidence Database identification of ELC2, conditional knockdown, molecular dynamics, point mutagenesis, gliding assays

    PMID:26374117

    Open questions at the time
    • Calcium-dependence of lever-arm stabilization based partly on simulation
    • Distinct roles of ELC1 vs ELC2 in vivo not delineated
  16. 2016 Medium

    A sequential motor handoff was defined whereby conoid-anchored MyoH first translocates the moving junction apically before IMC-anchored MyoA relays force for pellicular gliding and invasion.

    Evidence Conditional MyoH disruption, immunofluorescence, invasion/egress assays, MyoH-MyoA epistasis

    PMID:26760042

    Open questions at the time
    • Molecular basis of the handoff transition unresolved
    • How the two motors coordinate temporally not measured
  17. 2017 High

    The structural logic of light-chain assembly on the neck was resolved: MLC1 clamps the MyoA neck at ~10 nM and cooperatively raises ELC1 affinity 49-fold, with ELC1 also engaging the converter and its EF-hand coordinating calcium.

    Evidence X-ray crystallography (1.85 Å), HDX-MS, ITC binding measurements

    PMID:28972141

    Open questions at the time
    • In-cell relevance of cooperative affinity increase not tested
    • Link to force transduction in the intact motor not demonstrated
  18. 2017 Medium

    The primary function of the actomyosin system was reframed toward attachment when mlc1/act1 cKO parasites failed to adhere under flow yet retained wildtype-speed residual motility.

    Evidence Conditional mlc1/act1 knockout, 3D motility assays, substrate attachment under flow

    PMID:28100223

    Open questions at the time
    • Force-generation versus attachment contributions not fully separated
    • Source of residual motility unidentified
  19. 2018 High

    The divergent motor-domain architecture underpinning both chemomechanical coupling and drug specificity was established by crystal structure, revealing a class-defining SH1/SH2 region and non-human solvent pockets, with HDX-MS linking phosphorylation to local motor stability.

    Evidence X-ray crystallography (2.6 Å), HDX-MS, in vitro motility with phosphorylation variants

    PMID:30348763

    Open questions at the time
    • Full ATPase-cycle conformational states not captured
    • Direct inhibitor-bound structure not provided here
  20. 2020 High

    Structures of ELC-MyoA trimeric sub-complexes showed ELCs induce secondary structure in MyoA to stiffen the lever arm, and, contrary to earlier inference, calcium binding does not alter ELC structure.

    Evidence X-ray crystallography of trimeric sub-complexes, biophysical analysis

    PMID:33051581

    Open questions at the time
    • Reconciliation of calcium's role across studies incomplete
    • Dynamics of lever-arm stiffening under load not measured
  21. 2020 Medium

    The mechanical output of the motor during locomotion was quantified, showing acto-MyoA drives traction and requires an apical anchoring adhesion that stores energy in the microtubule cytoskeleton to set thrust for helical gliding.

    Evidence Traction force microscopy, reflection interference microscopy, micropatterning, expansion microscopy

    PMID:32432851

    Open questions at the time
    • Molecular identity of the apical adhesion not defined
    • Direct force per motor not resolved
  22. 2023 High

    MyoA was validated as a druggable in vivo target by KNX-002, which inhibits its actin-activated ATPase with vertebrate selectivity and whose on-target action was confirmed by a T130A resistance mutation and disease slowing in mice.

    Evidence HTS ATPase screen, chemical mutagenesis/selection, sequencing, in vitro motility, mouse infection with WT vs T130A

    PMID:37155705

    Open questions at the time
    • Structural mode of KNX-002 binding not resolved
    • Efficacy against chronic/bradyzoite stages not addressed
  23. 2024 Medium

    A role beyond motility was established: MyoA accumulates around the mitochondrion during division and is required for normal mitochondrial morphology and inheritance into daughter buds.

    Evidence Ultrastructure expansion microscopy, conditional MyoA knockdown, mitochondrion inheritance assays, actin pulldown with mitochondrion vesicles, yeast two-hybrid (LMF1-MyoA)

    PMID:39374269

    Open questions at the time
    • Direct LMF1-MyoA interaction based on Y2H not orthogonally validated
    • Whether the glideosome or a distinct MyoA pool drives inheritance unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
ACTIN/ACT1 (TRACK FOR MOTOR)ELC1 / ELC2 (ESSENTIAL LIGHT CHAINS, LEVER ARM)GAP40 (POLYTOPIC IMC PROTEIN)GAP45 (GLIDEOSOME-ASSOCIATED, RECRUITS MLC1-MYOA TO IMC)GAP50 (INTEGRAL IMC MEMBRANE ANCHOR)LMF1 (YEAST TWO-HYBRID INTERACTOR, MITOCHONDRION)MLC1 (MYOSIN LIGHT CHAIN, DIRECT BINDING PARTNER)MYOC (COMPENSATORY GLIDEOSOME MYOSIN)MYOH (SEQUENTIAL MOTOR RELAY PARTNER)TGCDPK3 (KINASE, PHOSPHORYLATES SER21/SER743)TGUNC (UCS-FAMILY CO-CHAPERONE REQUIRED FOR FOLDING)
Complex memberships
Glideosome (MyoA-MLC1-GAP45-GAP50, with GAP40)MyoA-MLC1-ELC1/ELC2 lever-arm complex

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 TgMyoA is a fast, single-headed, plus-end-directed motor that moves actin filaments in unitary steps of 5.3 nm at a velocity of 5.2 µm/s, as established by microneedle-laser trap and sliding velocity assays. TgMyoA binds a novel myosin light chain TgMLC1 and is anchored at the plasma membrane. In vitro motility assay, microneedle-laser trap (optical tweezers), biochemical characterization of purified motor complex The EMBO journal High 11980712
2002 Conditional removal of MyoA using a tetracycline-inducible system caused severe impairment in host cell invasion and parasite spreading in cultured cells, and established MyoA as essential for pathogenesis in an animal model. Tetracycline-inducible conditional gene disruption (regulatable transactivator system), cell invasion assays, animal model infection Science High 12399593
2001 Overexpression of a MyoA transgene drastically down-regulates the level of endogenous MyoA, indicating MyoA is under tight feedback regulation at the protein level. Tetracycline-inducible expression system, Western blot analysis of endogenous protein levels Nucleic acids research Medium 11713335
2004 TgMyoA forms a protein complex with its light chain TgMLC1 and two novel proteins TgGAP45 and TgGAP50. This complex is localized to the inner membrane complex, where it is anchored by TgGAP50, an integral membrane glycoprotein. Complex assembly is spatially controlled and occurs in two stages. Co-immunoprecipitation, subcellular fractionation, immunofluorescence localization, identification of novel complex components The Journal of cell biology High 15123738
2010 The glideosome contains MyoA, MLC1, GAP45, GAP50, and a newly identified polytopic IMC protein GAP40. GAP45 is anchored to the plasma membrane and IMC via its N- and C-terminal extremities respectively; its C-terminal region recruits MLC1-MyoA to the IMC. GAP45 is essential for gliding, invasion, and egress. Conditional knockdown, co-immunoprecipitation, immunofluorescence, complementation experiments including transgenera complementation with P. falciparum GAP45 Cell host & microbe High 20951968
2008 Phosphorylation of GAP45 at Ser163 and Ser167 controls the final step of MyoA motor complex assembly: phosphomimetic mutations (Ser-to-Glu) prevent association of the MyoA-MLC1-GAP45 subcomplex with the membrane anchor GAP50, while alanine mutations do not affect assembly. Mass spectrometry identification of phosphorylation sites, site-directed mutagenesis (Ser-to-Glu and Ser-to-Ala), co-immunoprecipitation Eukaryotic cell High 19047362
2011 Calcium-dependent phosphorylation of six residues across GAP45, MLC1, and MyoA correlates with invasion motor activity. A novel 15-kDa calmodulin-like protein (MyoA Essential Light Chain) associates more strongly with the invasion motor upon calcium stimulation, identifying a new regulatory component. SILAC-based quantitative LC-MS/MS phosphoproteomics, 2-DE of 32P-labeled protein extracts, calcium stimulation experiments PLoS pathogens Medium 21980283
2010 Post-translational modification of TgMLC1 by a small-molecule inhibitor (tachyplegin) causes decreased TgMyoA motor activity, as shown by in vitro motility assay comparing motor complexes from treated vs. untreated parasites. This established that Class XIV myosin motor activity can be modulated by PTMs on its associated light chain. In vitro motility assay with purified motor complexes, electrophoretic mobility shift, peptide mapping PLoS pathogens High 20084115
2014 TgMyoA undergoes calcium-dependent phosphorylation; a small-molecule enhancer of motility (compound 130038) causes increased intracellular calcium leading to increased TgMyoA phosphorylation. Parasites expressing nonphosphorylatable mutant MyoA egressed from host cells more slowly in response to calcium ionophore, demonstrating that calcium-dependent phosphorylation of MyoA modulates myosin-driven processes. Site-directed mutagenesis of phosphorylation sites, calcium ionophore treatment, egress assays, compound treatment, intracellular calcium measurement Molecular biology of the cell High 24989796
2015 TgCDPK3 phosphorylates TgMyoA at Ser21 and Ser743 in vitro. Complementation of a myoA null mutant with MyoA bearing S21A or S743A alanine mutations failed to rescue the egress delay phenotype, while phosphomimetic mutations bypassed the need for TgCDPK3. This establishes TgCDPK3-mediated phosphorylation of TgMyoA as the mechanism for rapid initiation of motility and egress. BioID proximity interaction screen, peptide array kinase assay in vitro, genetic complementation with phosphomimetic/alanine mutants, egress assays PLoS pathogens High 26544049
2014 MyoA and its associated motor complex (MLC1, GAP45, Act1) are important but not absolutely essential for gliding motility and host cell invasion; conditional KO mutants remain invasive, suggesting alternative invasion mechanisms exist alongside the MyoA-glideosome. Conditional knockout of MyoA, MLC1, GAP45, Act1; invasion and motility assays PloS one Medium 24632839
2014 Deletion of MyoA leads to relocalization of MyoC along the pellicle and at the apical cap, accounting for residual invasion. MyoA and MyoC glideosomes exhibit plasticity, with MyoC-glideosome providing functional compensation for loss of MyoA. Conditional knockout of MyoA, immunofluorescence localization of MyoC, invasion assays PLoS pathogens Medium 25393004
2015 Two essential light chains (ELC1 and ELC2) bind the MyoA lever arm and are functionally redundant but important for invasion, egress, and motility. Ca2+ promotes intermolecular contacts between ELCs and the adjacent MLC1 to stabilize the lever arm domain, as demonstrated by point mutations predicted to ablate Ca2+ binding or the ELC-MLC1 interface. Identification of ELC2 by database search, conditional knockdown, molecular dynamics simulations, point mutagenesis, gliding motility assays mBio Medium 26374117
2014 TgMyoA expressed in Sf9 cells requires a parasite-specific UCS-family co-chaperone (TgUNC) to be soluble and functional. The MyoA heavy chain with only MLC1 moves actin at ~1.5 µm/s, but addition of ELC1 increases speed to ~3.4 µm/s, demonstrating that two light chains bound to the lever arm are required for fast motility. Baculovirus/Sf9 heterologous expression, in vitro actin gliding motility assay, co-expression of chaperone and light chains The Journal of biological chemistry High 25231988
2018 The 2.6-Å crystal structure of the TgMyoA motor domain reveals a divergent SH1/SH2 region and class-defining 'HYAG'-site polymorphism as key structural elements for force transduction and chemomechanical coupling. Hydrogen-deuterium exchange MS showed that phosphorylation-dependent enhanced motility correlates with increased local stability in specific regions of the motor. Solvent-accessible pockets differ from human myosins, supporting inhibitor design. X-ray crystallography (2.6 Å), hydrogen-deuterium exchange coupled to MS, in vitro motility assay with phosphorylation variants Proceedings of the National Academy of Sciences of the United States of America High 30348763
2017 MLC1 and ELC1 bind adjacent sites on the MyoA neck (residues 775–818). The 1.85-Å crystal structure of MLC1 bound to its MyoA peptide shows a bilobed architecture with MLC1 clamping around the helical peptide (Kd ~10 nM). Ca2+ coordination by an EF-hand in ELC1 and pre-binding of MLC1 cooperate to increase ELC1 affinity for the neck 49-fold, to ~12 nM. ELC1 also engages the MyoA converter subdomain. X-ray crystallography (1.85 Å), hydrogen-deuterium exchange MS, isothermal titration calorimetry, binding affinity measurements The Journal of biological chemistry High 28972141
2020 Crystal structures of ELC in trimeric sub-complexes with MyoA show that ELCs bind a conserved MyoA sequence and induce secondary structure in MyoA to stiffen its lever arm. Structural and biophysical analysis reveals that calcium binding has no influence on ELC structure. X-ray crystallography of trimeric sub-complexes, biophysical analysis (SPR/ITC) Communications biology High 33051581
2016 MyoH is indispensable for translocation of the circular junction from the parasite tip to the apical IMC position; once this first step is accomplished, MyoA relays the process to enact effective gliding and invasion along the pellicle. This establishes a sequential handoff between MyoH (conoid-anchored) and MyoA (IMC-anchored) during motility. Conditional disruption of TgMyoH, immunofluorescence, invasion and egress assays, epistasis between MyoH and MyoA PLoS pathogens Medium 26760042
2017 Parasites with mlc1 cKO (and act1 cKO) are virtually unable to attach to a collagen-coated substrate under flow conditions while retaining residual motility at wildtype speed, demonstrating that the actomyosin system (including MyoA via MLC1) functions primarily in surface attachment rather than as the sole force generator for movement. Conditional knockout of mlc1 and act1, 3D motility assays, substrate attachment assays under flow, comparison of mutant phenotypes BMC biology Medium 28100223
2014 TgMLC1 C58 is the direct covalent target of tachypleginA and its analogues, as demonstrated by click chemistry labelling. A C58S recombinant TgMLC1 mutation is refractory to compound binding, and knock-in parasites expressing C58S show decreased sensitivity to compound-induced motility inhibition, confirming TgMLC1 as the mechanistic target mediating inhibition of TgMyoA motor activity. Click chemistry labelling with alkyne-derivatized inhibitor, site-directed mutagenesis (C58S, S57A), knock-in parasite line, 3D motility assay PloS one High 24892871
2023 A small-molecule inhibitor KNX-002 inhibits TgMyoA actin-activated ATPase activity in vitro with little effect on vertebrate myosins. A resistance mutation T130A in TgMyoA reduces compound sensitivity both in biochemical and parasite assays, validating TgMyoA as a druggable target in vivo and establishing that KNX-002 slows disease progression in mice through on-target MyoA inhibition. High-throughput screen of 50,000 compounds for ATPase inhibition, chemical mutagenesis + selection, targeted sequencing, in vitro motility assay, mouse infection model with wild-type vs. T130A parasites PLoS biology High 37155705
2024 MyoA accumulates around the mitochondrion in late stages of parasite division (ultrastructure expansion microscopy). Parasites lacking MyoA show defective mitochondrial morphology and delay in mitochondrion delivery to daughter buds during division, establishing a role for MyoA in organellar inheritance beyond gliding motility. Mitochondrion vesicles extracted from parasites interact with actin filaments. Ultrastructure expansion microscopy (U-ExM), conditional MyoA knockdown, mitochondrion morphology and inheritance assays, actin pulldown with mitochondrion vesicles, yeast two-hybrid (LMF1-MyoA interaction identified) PLoS pathogens Medium 39374269
2020 The acto-MyoA motor directs traction force during tachyzoite helical gliding; traction force microscopy and reflection interference microscopy revealed a critical apical anchoring adhesion that stores energy via microtubule cytoskeleton and sets thrust force for helical gliding. Quantitative traction force microscopy, reflection interference microscopy, micropatterning, expansion microscopy ACS nano Medium 32432851

Source papers

Stage 0 corpus · 29 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion. Science (New York, N.Y.) 399 12399593
2010 Functional dissection of the apicomplexan glideosome molecular architecture. Cell host & microbe 234 20951968
2004 Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii. The Journal of cell biology 214 15123738
2002 Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor. The EMBO journal 197 11980712
2001 Modulation of myosin A expression by a newly established tetracycline repressor-based inducible system in Toxoplasma gondii. Nucleic acids research 116 11713335
2014 The toxoplasma Acto-MyoA motor complex is important but not essential for gliding motility and host cell invasion. PloS one 91 24632839
2017 Surface attachment, promoted by the actomyosin system of Toxoplasma gondii is important for efficient gliding motility and invasion. BMC biology 81 28100223
2014 Plasticity between MyoC- and MyoA-glideosomes: an example of functional compensation in Toxoplasma gondii invasion. PLoS pathogens 77 25393004
2016 The Conoid Associated Motor MyoH Is Indispensable for Toxoplasma gondii Entry and Exit from Host Cells. PLoS pathogens 75 26760042
2011 Quantitative in vivo analyses reveal calcium-dependent phosphorylation sites and identifies a novel component of the Toxoplasma invasion motor complex. PLoS pathogens 73 21980283
2003 Toxoplasma gondii: perfecting an intracellular life style. Traffic (Copenhagen, Denmark) 73 12911812
2015 Phosphorylation of a Myosin Motor by TgCDPK3 Facilitates Rapid Initiation of Motility during Toxoplasma gondii egress. PLoS pathogens 70 26544049
2008 GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex. Eukaryotic cell 65 19047362
2015 Two Essential Light Chains Regulate the MyoA Lever Arm To Promote Toxoplasma Gliding Motility. mBio 40 26374117
2010 A small-molecule inhibitor of T. gondii motility induces the posttranslational modification of myosin light chain-1 and inhibits myosin motor activity. PLoS pathogens 39 20084115
2014 Calcium-dependent phosphorylation alters class XIVa myosin function in the protozoan parasite Toxoplasma gondii. Molecular biology of the cell 36 24989796
2014 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 36 25231988
2020 Coupling Polar Adhesion with Traction, Spring, and Torque Forces Allows High-Speed Helical Migration of the Protozoan Parasite Toxoplasma. ACS nano 34 32432851
2011 Unusual anchor of a motor complex (MyoD-MLC2) to the plasma membrane of Toxoplasma gondii. Traffic (Copenhagen, Denmark) 28 21143563
2020 Structural role of essential light chains in the apicomplexan glideosome. Communications biology 17 33051581
2018 Structural and mechanistic insights into the function of the unconventional class XIV myosin MyoA from Toxoplasma gondii. Proceedings of the National Academy of Sciences of the United States of America 16 30348763
2017 Dissecting the molecular assembly of the Toxoplasma gondii MyoA motility complex. The Journal of biological chemistry 16 28972141
2014 Identification of T. gondii myosin light chain-1 as a direct target of TachypleginA-2, a small-molecule inhibitor of parasite motility and invasion. PloS one 16 24892871
2006 Functional and biophysical analyses of the class XIV Toxoplasma gondii myosin D. Journal of muscle research and cell motility 14 16470333
2023 MyosinA is a druggable target in the widespread protozoan parasite Toxoplasma gondii. PLoS biology 11 37155705
2021 Blocking Palmitoylation of Toxoplasma gondii Myosin Light Chain 1 Disrupts Glideosome Composition but Has Little Impact on Parasite Motility. mSphere 11 34011689
2024 Myosin A and F-Actin play a critical role in mitochondrial dynamics and inheritance in Toxoplasma gondii. PLoS pathogens 4 39374269
2024 Myosin A and F-Actin play a critical role in mitochondrial dynamics and inheritance in Toxoplasma gondii. bioRxiv : the preprint server for biology 1 38562694
2023 Knocking down the expression of the molecular motors, myosin A, C and F genes in Toxoplasma gondii to decrease the parasite virulence. Experimental parasitology 0 37331576