A number of cellular control mechanisms have evolved that facilitate and evaluate post-translational steps in protein biosynthesis. Chaperones or escort proteins are an important part of these cellular control mechanisms. They associate with newly synthesized proteins and assure correct folding and post-translational modification including disulfide bridge formation, glycosylation and complex formation. The receptor-associated protein (RAP) is a novel type of chaperone recently identified that is especially designed to assist in the biosynthesis and intracellular transport of endocytic receptors. Experimental evidence suggests that RAP acts as a receptor antagonist and prevents association of newly synthesized receptors with their ligands during transport to the cell surface. This mechanism seems to be required in cell types that express both receptor and ligand because premature receptor-ligand interaction in the secretory pathway interferes with proper export of the receptors to the cell surface. This review describes studies that have uncovered this unique protein biosynthesis mechanism.