Malaria is a mosquito-borne parasitic disease responsible for more than half a million deaths per year, the majority being children. The causative agents of this disease are Apicomplexan parasites from the genus Plasmodium. Despite intensive research efforts and funds invested to fight malaria, Plasmodium parasites are developing resistances to all the existing treatments. There is an urgent need for the identification of novel pharmaceutical targets in order to develop a new generation of antimalarial treatments. Recent studies on the complex lifecycle of Apicomplexan parasites have demonstrated the essentiality of a macromolecular complex, the glideosome, for parasite motility and invasion. This complex is organized around a divergent actomyosin complex containing the atypical myosin A (MyoA) and short and unstable filaments of actin 1 (Act1). Our work on Plasmodium falciparum MyoA (PfMyoA) shows how an unforeseen phosphorylatable N-terminal extension can tune the force produced by the motor and adapt it to the different stages of Plasmodium. Interestingly, conditional knock-out of PfMyoA demonstrates that PfMyoA is essential for red blood cell invasion by the parasite.  These results, along with the high-resolution structure of the PfMyoA/PfAct1 system solved by cryo-electron microscopy, allow us to describe how the glideosome produces the force necessary for host-cell invasion. Ultimately, the more recent study of KNX-002, a first-in-class inhibitor of PfMyoA, confirms that the glideosome is a promising pharmaceutical target.