To the malaria parasite, the prospect of setting up residence within a human erythrocyte represents a formidable challenge. The mature human erythrocyte is essentially a bag of haemoglobin with no internal organelles and no protein synthesis machinery. The parasite needs, therefore, to assemble all the essential amenities--foundations, plumbing and furnishings--from scratch. The parasite remodels its adopted home by exporting proteins to the erythrocyte membrane. To reach their final destinations, the exported proteins must cross the parasite plasma membrane, the parasitophorous vacuole membrane and the erythrocyte cytosol. To further understand this unusual and complex trafficking pathway, we have searched for proteins that may form part of the trafficking machinery of the infected erythrocyte. We have identified an ER-located, calcium-binding homologue of reticulocalbin (PfERC) that co-localizes with the ER molecular chaperone, PfGRP. We have also identified a homologue of the GTP-binding protein, Sar1p, a small GTPase that, in other eukaryotic cells, is thought to play a crucial role in trafficking proteins between the ER and the Golgi. PfSar1p is located in discrete structures near the periphery of the parasite cytoplasm that may represent specialized export compartments. PfSar1p is exported to structures outside the parasite in the erythrocyte cytoplasm. The malaria parasite appears to be capable of elaborating components of the 'classical' vesicle mediated trafficking machinery outside the boundaries of its own plasma membrane.