The apicoplast is a relict plastid of cyanobacterial origin found in most apicomplexan parasites, including P. falciparum. The apicoplast can be selectively targeted by antibiotic- and herbicide-like drugs and treatment of asexual P. falciparum with such inhibitors causes a peculiar ‘delayed death’ phenotype, where treated parasites arrest in the subsequent intraerythrocytic development cycle. Despite the widespread use of such drugs as malaria prophylactics (e.g. doxycycline), the molecular basis of delayed death has not been thoroughly described. Understanding these mechanisms will assist in informing appropriate clinical usage of apicoplast inhibitors. The apicoplast is responsible for the biosynthesis of isoprenoid precursors, which have at least three downstream fates in the Plasmodium parasite: protein prenylation, ubiquinone and dolichols. The effect of protein prenylation and ubiquinone loss in the parasite has been previously described, but the effect of dolichol loss has not been characterised. Dolichols are required for the biosynthesis of glycosylphosphatidylinositol (GPI) anchors, the predominant type of protein glycosylation present in P. falciparum. Many GPI-anchored proteins are thought to be essential for both parasite egress and reinvasion. We performed immunofluorescence assays and electron microscopy on P. falciparum with inhibited apicoplasts but with exogenous rescue of their prenylation depletion. In these parasites, GPI-anchored proteins become mis-localised from their normal membrane association. These GPI-anchorless parasites also exhibited an egress defect and are unable to undergo proper segmentation and rupture the parasitophorous vacuole. Through flow cytometry‑based invasion assays, we found that these GPI-anchorless parasites are also substantially less invasive. Therefore, our data indicates that apicoplast inhibitors cause a defect in GPI anchor biosynthesis that is important for both egress and reinvasion of asexual-stage P. falciparum.