Abstract
RETENTION of resident proteins in the lumen of the endoplasmic reticulum is achieved in both yeast and animal cells by their continual retrieval from the cis-Golgi, or a pre-Golgi compartment1–3. Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually Lys-Asp-Glu-Leu (KDEL in the single letter code) in animal cells, His-Asp-Glu-Leu (HDEL) in Sac-charomyces cerevisiae2,4,5. There is evidence that the ERD2 gene encodes the sorting receptor that recognizes HDEL in yeast6,7; its product is an integral membrane protein of relative molecular mass 26,000 (26K) that is not glycosylated. In contrast, Vaux et al.8 suggest that the mammalian KDEL receptor is a 72K gly-coprotein that they detected using an anti-idiotypic antibody approach. If this were so, it would indicate a surprising divergence of the retrieval machinery between yeast and animal cells. We report here that human cells express a protein similar in sequence, size and properties to the ERD2 product, and propose that this protein is the human KDEL receptor.
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Lewis, M., Pelham, H. A human homologue of the yeast HDEL receptor. Nature 348, 162–163 (1990). https://doi.org/10.1038/348162a0
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DOI: https://doi.org/10.1038/348162a0
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