Members of the LDL receptor gene family mediate cellular uptake of various extracellular ligands, including lipoprotein particles. Ligand interactions with these receptors can be antagonized by a 39 kDa receptor-associated protein. Recent biochemical, cellular, and genetic studies have shown that receptor-associated protein is a molecular chaperone/escort protein for LDL receptor-related protein, a member of the LDL receptor gene family that binds multiple ligands. These studies indicate that receptor-associated protein interacts with LDL receptor-related protein at multiple sites and assists the proper folding and disulfide bond formation of LDL receptor-related protein within the endoplasmic reticulum. Following the completion of folding, receptor-associated protein remains associated with the receptor during its subsequent trafficking along the early secretory pathway, thereby preventing premature ligand interaction with the receptor. The ability of receptor-associated protein to universally inhibit ligand interactions with members of the LDL receptor gene family underscores the use of this protein as a tool in the study of ligand-receptor interactions.