Abstract
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.
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CITATION STYLE
Bu, G., & Schwartz, A. L. (1998, December 1). RAP a novel type of ER chaperone. Trends in Cell Biology. Elsevier Ltd. https://doi.org/10.1016/S0962-8924(98)01283-5
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