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. 2019 Jul 23;10:3286. doi: 10.1038/s41467-019-11120-0

Fig. 6.

Fig. 6

Phosphorylation of PfMyoA tunes its motor properties. Scheme representing how phosphorylation tunes PfMyoA motor properties and how this could optimize the motor for parasite motility or invasion at different stages of the parasite. In highly motile stages, sporozoites move at a speed higher than 2 µm/s. At this stage, phosphorylation of PfMyoA would allow the parasite to move actin at maximal speed but with low ensemble force. In merozoites, which lack continuous motility, but are instead adapted for erythrocyte invasion, dephosphorylation of PfMyoA localized at the invasion junction would result in active motors efficient in invasion. This merozoite PfMyoA motor would spend more of its total cycle time strongly bound to actin, thereby resulting in greater ensemble force output. The apparent duty ratio in the two phosphorylation states was estimated from the rate of ADP release divided by the total ATPase cycle time. The S19A, K764E and ∆N mutants would likely impair speed but not invasion, because their ensemble force is higher than phosphorylated, wild-type PfMyoA. Phosphorylation of the N-term extension of PfMyoA can thus act as a switch to tune motor activity depending on the needs of the parasite (high speed and low force for gliding, or higher force for the low speed invasion process)