The cell surface is the main interface between many parasites and their human hosts, making surface proteins an important target in the fight against parasitic diseases. In the African parasite Trypanosoma brucei, many of these proteins are anchored to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor. These proteins play vital cellular roles and are found in different surface domains. Yet their sorting mechanism remains unknown. Previous studies suggested the involvement of GPI anchors in protein sorting. If true, I hypothesise that the key to correct trafficking lies within the protein's C-terminal GPI insertion site (Ct). Until recently, only two GPI-anchored proteins (VSG and TfR) have been reported in T.brucei. Thanks to a recent proteomic study, a large set of GPI-anchored surface proteins is now available for investigation. To test my hypothesis, the Ct sequences of a subset of proteins of known cellular localisation was fused to a GFP ORF, and the localisation of these derivatives was analysed by native fluorescence microscopy. Results show a correlation between GFP-derivatives and their respective proteins, suggesting that the GPI insertion signal does play a role in the sorting of GPI-anchored proteins.