A human homologue of the yeast HDEL receptor

Nature. 1990 Nov 8;348(6297):162-3. doi: 10.1038/348162a0.


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 compartment. 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 Saccharomyces cerevisiae. There is evidence that the ERD2 gene encodes the sorting receptor that recognizes HDEL in yeast; its product is an integral membrane protein of relative molecular mass 26,000 (26K) that is not glycosylated. In contrast, Vaux et al. suggest that the mammalian KDEL receptor is a 72K glycoprotein 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.

MeSH terms

  • Amino Acid Sequence
  • Cell Compartmentation
  • Cloning, Molecular
  • Golgi Apparatus / metabolism
  • Humans
  • Kluyveromyces / genetics
  • Membrane Proteins / genetics*
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Receptors, Cell Surface / physiology*
  • Receptors, Peptide*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins*
  • Solubility
  • Transfection


  • ERD2 protein, S cerevisiae
  • KDELR1 protein, human
  • Membrane Proteins
  • Receptors, Cell Surface
  • Receptors, Peptide
  • Saccharomyces cerevisiae Proteins

Associated data

  • GENBANK/X55885