The malaria parasite Plasmodium falciparum modifies the host red blood cell (RBC) for survival. This remodelling is facilitated by the export of many parasite proteins into the RBC cytoplasm. Some of these proteins, including the major virulence protein PfEMP1, are exported via an intermediate trafficking structure called Maurer’s clefts. The final steps in the transfer of PfEMP1 to the RBC membrane from the cleft are poorly understood. Previous electron tomography studies of the parasite have revealed tether-like structures connecting Maurer’s clefts to the RBC membrane. These tethers have been hypothesised to play a role in immobilising the Maurer’s clefts at the RBC membrane, where they may function in the final steps of PfEMP1 trafficking and surface display. MAHRP2 is the only protein currently known to localise to the tether. Immunoprecipitation studies of MAHRP2-GFP revealed several new proteins. Here we report on one of these proteins termed the MAHRP2 interacting protein (MIP). MIP localises to the Maurer’s clefts and conditional knockdown studies show that MIP is required for parasite adhesion to endothelial receptors and that deletion of MIP leads to a delay in the immobilisation of the Maurer’s clefts to the RBC membrane.