The addition of glycophosphatidylinositol (GPI) anchors represents an important post-translational modification which enables proteins associate with biological membranes and is the predominant glycoconjugate in Plasmodium parasites. During the intraerythrocytic asexual cycle the GPI-anchored proteome is predominantly expressed in the later trophozoite and schizont stages and is almost exclusively localised to the merozoite surface where they constitute greater than 50% of the total surface protein coat. Notable among these is merozoite surface protein 1 (MSP1), which has an established function in egress whereby it contributes to the destabilization of the host red blood cell cytoskeleton, leading to cell rupture and the release of daughter parasites. An essential component to GPIs is the sugar residue mannose which is donated by dolichol-phosphate in the endoplasmic reticulum. Dolichols themselves are believed to derive from isoprenoid precursors synthesised in the Plasmodium apicoplast, a relict plastid organelle of Prokaryotic origin. We found that treatment of Plasmodium parasites with apicoplast inhibitors decreases the abundance of isoprenoid and GPI intermediates resulting in GPI-anchored proteins becoming untethered from their normal membrane association. This detachment results in the mis-localisation of surface GPI-anchored proteins to the parasitophorous vacuole. Following the loss of surface bound MSP1, these GPI-deficient parasites experienced an egress defect, though surprisingly also exhibited aberrant membrane morphology and unsuccessful segmentation. Our data provides further evidence for the importance of GPI biosynthesis during the asexual cycle of P. falciparum, and indicates that GPI biosynthesis, and in extension egress, is dependent on isoprenoids synthesised in the apicoplast.