Protein disulfide isomerase: A multifunctional protein of the endoplasmic reticulum

  • J. M. Luz
  • W. J. Lennarz
Part of the EXS book series (EXS, volume 77)


Protein disulfide isomerase (PDI) is a resident enzyme of the endoplasmic reticulum (ER) that was discovered over three decades ago. Contemporary biochemical and molecular biology techniques have revealed that it is present in all eukaryotic cells studied and retained in the ER via a -KDEL or -HDEL sequence at its C-terminus. However, evidence is accumulating that, in certain cell types, PDI can be found in other subcellular compartments, despite possessing an intact retention sequence. A wide range of studies has established that in presence of a redox pair, PDI acts catalytically to both form and reduce disulfide bonds, therefore acting as a disulfide isomerase. Recent studies have focused on the mechanism of the isomerization process and the precise role of the two active site sequences (-CGHC-) in the process. In addition, prokaryotes have been shown to possess a set of proteins that function in a similar fashion, being able to generate disulfide bonds on polypeptides translocated into the periplasmic space. Following the recent discovery that PDI binds peptides, coupled with earlier findings that PDI is a subunit of at least two enzymatic complexes (prolyl 4-hydroxylase and microsomal triglyceride transfer protein), it seems that it may serve functions other than merely that of a disulfide isomerase. In fact, it is now clear that PDI can facilitate protein folding independently of its disulfide isomerase activity. A major challenge for the future is to define mechanistically how it accomplishes isomerization and the relationship between this process and the protein folding steps that culminate in the final, fully mature protein.


Disulfide Bond Multifunctional Protein Disulfide Bond Formation Microsomal Triglyceride Transfer Protein Endoplasmic Reticulum Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Birkhäuser Verlag Basel/Switzerland 1996

Authors and Affiliations

  • J. M. Luz
    • 1
  • W. J. Lennarz
    • 1
  1. 1.Department of Biochemistry and Cell BiologyState University of New York at Stony BrookStony BrookUSA

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