Apicomplexan parasites possess a highly conserved molecular motor associated to motility. This machinery, called the glideosome, is structured around the acylated Gliding-Associated Protein GAP45 that recruits myosin A (MyoA) and its associated Myosin Light Chains (MLC1). To determine if previously mapped phosphorylation sites on TgGAP45 and TgMLC1 have a direct significance for the glideosome, series of phospho-mutants were generated. Despite the extensive phosphorylation of TgMLC1 and TgGAP45, phosphorylation does not appear to be critical for the glideosome function. Apicomplexan parasites possess a plastid-like organelle called the apicoplast. We demonstrated that apicoplast inheritance is an actin-based process. Conditional knockdown of the conserved TgMyoF severely impacts on apicoplast turnover leading to parasite death. We also conditionally stabilized the tail of MyoF, which forms an inactive heterodimer with endogenous TgMyoF. This dominant negative mutant reveals a central role of this motor in the positioning of the two centrosomes prior to daughter cell formation.