Members of the low-density lipoprotein (LDL) receptor gene family play an important role in cellular uptake of various extracellular ligands. Recent studies have shown that a 39-kDa protein known as RAP (receptor-associated protein) serves as a molecular chaperone to assist the folding of certain LDL-receptor family proteins and their passage through the secretory pathway. In this review, the authors discuss our current understanding of the roles of RAP as a molecular chaperone/escort protein and present a model of how RAP might carry out these functions.