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Related Experiment Videos

Sequence of a second human KDEL receptor.

M J Lewis1, H R Pelham

  • 1MRC Laboratory of Molecular Biology, Cambridge, U.K.

Journal of Molecular Biology
|August 20, 1992
PubMed
Summary

Scientists discovered a second human gene encoding KDEL receptors, crucial for retaining endoplasmic reticulum (ER) proteins. This finding reveals at least two distinct proteins responsible for this vital cellular retrieval process.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Trafficking

Background:

  • Endoplasmic reticulum (ER) proteins are retained via a C-terminal tetrapeptide signal.
  • This signal mediates retrieval from later secretory pathway compartments.
  • A receptor molecule, cycling between the Golgi and ER, recognizes this signal.

Purpose of the Study:

  • To identify and characterize human homologues of the yeast ERD2 gene.
  • To investigate the function of human KDEL receptors in protein retention.
  • To determine if multiple KDEL receptors exist in humans.

Main Methods:

  • Isolation of human cDNA homologous to the yeast ERD2 gene.
  • Characterization of the binding properties and cellular localization of the encoded protein.
  • Identification of a related human protein with similar functional properties.

Main Results:

  • A human cDNA homologue of the yeast ERD2 gene was isolated.
  • The human KDEL receptor product shifts from the Golgi to the ER upon ligand binding, indicating triggered retrograde transport.
  • A second, related human protein with similar properties was identified.

Conclusions:

  • There are at least two distinct genes in humans encoding functional KDEL receptors.
  • These receptors play a critical role in the retrieval of ER-resident proteins.
  • Understanding KDEL receptor function is key to comprehending protein trafficking and retention in the secretory pathway.

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