Analysis of the retention signals of two resident luminal endoplasmic reticulum proteins by in vitro mutagenesis

S. M. Haugejorden, M. Srinivasan, M. Green

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

Protein disulfide isomerase (PDI, ERp59), ERp72, and ERp61 are luminal proteins of the endoplasmic reticulum (ER) that are characterized by the presence of sequences corresponding to the active site regions of PDI. Each one of these proteins possesses a different COOH-terminal tetrapeptide ER retention signal. In order to investigate what other tetrapeptide sequences could serve as retention signals and to determine to what extent the function of the retention signal is modulated by the protein carrying the signal, we have constructed a set of mutants of two of these resident ER proteins, PDI and ERp72. In each of these proteins, the wild type tetrapeptide sequences were replaced by each member of the set of the 12 possible combinations consisting of (K,R,Q)-(D,E)-(D,E)-L. Analysis of the efficiency of retention of the variant proteins when each was transiently expressed in COS cells showed that the retention efficiencies vary with both the COOH-terminal sequence and with the protein that carries this sequence.

Original languageEnglish
Pages (from-to)6015-6018
Number of pages4
JournalJournal of Biological Chemistry
Volume266
Issue number10
StatePublished - Jul 23 1991
Externally publishedYes

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