pH-dependent binding of KDEL to its receptor in vitro

Duncan W. Wilson, Michael J. Lewis, Hugh R B Pelham

Research output: Contribution to journalArticle

147 Citations (Scopus)

Abstract

The erd2 protein is the receptor responsible for recycling proteins bearing the carboxyl-terminal sequence KDEL (single-letter amino acid code) to the endoplasmic reticulum, following their loss from that organelle by the process of forward transport. To study the interaction of erd2p with the sequence KDEL we have reconstituted binding of erd2p to its ligand in vitro. Binding in vitro exhibits the same sequence specificity as retention of lumenal proteins in vivo and is strikingly sensitive to pH. Our results raise the possibility that erd2p-mediated sorting of lumenal endoplasmic reticulum proteins is facilitated by the pH differences between compartments of the secretory pathway.

Original languageEnglish (US)
Pages (from-to)7465-7468
Number of pages4
JournalJournal of Biological Chemistry
Volume268
Issue number10
StatePublished - Apr 5 1993
Externally publishedYes

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lysyl-aspartyl-glutamyl-leucine
Endoplasmic Reticulum
Proteins
Bearings (structural)
Secretory Pathway
Sorting
Organelles
Recycling
Ligands
Amino Acids
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry

Cite this

Wilson, D. W., Lewis, M. J., & Pelham, H. R. B. (1993). pH-dependent binding of KDEL to its receptor in vitro. Journal of Biological Chemistry, 268(10), 7465-7468.

pH-dependent binding of KDEL to its receptor in vitro. / Wilson, Duncan W.; Lewis, Michael J.; Pelham, Hugh R B.

In: Journal of Biological Chemistry, Vol. 268, No. 10, 05.04.1993, p. 7465-7468.

Research output: Contribution to journalArticle

Wilson, DW, Lewis, MJ & Pelham, HRB 1993, 'pH-dependent binding of KDEL to its receptor in vitro', Journal of Biological Chemistry, vol. 268, no. 10, pp. 7465-7468.
Wilson, Duncan W. ; Lewis, Michael J. ; Pelham, Hugh R B. / pH-dependent binding of KDEL to its receptor in vitro. In: Journal of Biological Chemistry. 1993 ; Vol. 268, No. 10. pp. 7465-7468.
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