Toxoplasma gondii is an obligate intracellular parasite belonging to the phylum Apicomplexa that can infect humans. This parasite developed a specific mechanism of invasion based on an apical complex and a mechanism of secretion. It has been observed that an apicomplexan specific methyltransferase (AKMT, Apical Lysine (K) Methyltransferase) was necessary for the mechanism of invasion, egress and motility of the parasite. More precisely, the methyltransferase activity of AKMT is essential to the apical localization of GAC (Glideosome Associated Connector). This latter connects the actomyosin system (called glideosome) with the micronemal adhesins. The moving junction (MJ) starts at the conoid and moves to the apical end of the inner membrane complex (IMC) due to the activity of the myosin H. after, the myosin A takes over from the apical end of the IMC to the basal end of the parasite. GAC is necessary for the mechanism of invasion, egress and motility, but was not demonstrated to be methylated. This study tries to identify the substrate(s) of AKMT responsible for the apical localization of GAC.