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PMID: 10085220 Published · ppublish English Journal Article Review

The protein disulphide-isomerase family: unravelling a string of folds.

The Biochemical journal ·Vol. 339 ( Pt 1) ·1999-04-01 ·Pages 1-10

Ferrari DM, Söling HD

Abstract

The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum. These proteins are characterized by the presence of one or more domains of roughly 95-110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing and one domain lacking a redox-active -Cys-Xaa-Xaa-Cys- tetrapeptide. In addition to their known roles as redox catalysts and isomerases, the last few years have revealed additional functions of the PDI proteins, including peptide binding, cell adhesion and perhaps chaperone activities. Attention is now turning to the non-redox-active domains of the PDIs, which may play an important role in all of the known activities of these proteins. Thus the presence of both redox-active and -inactive domains within these proteins portends a complexity of functions differentially accommodated by the various family members.

MeSH Terms
Carboxypeptidases/metabolism Cathepsin A Models, Chemical Molecular Chaperones/metabolism Oxidation-Reduction Protein Disulfide-Isomerases/metabolism Protein Folding Saccharomyces cerevisiae/enzymology Thioredoxins/metabolism
Chemicals
Molecular Chaperones Thioredoxins Carboxypeptidases Cathepsin A Protein Disulfide-Isomerases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ferrari D M
Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, D37077 Göttingen, Germany. dferrar@gwdg.de
Söling H D
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Email
dferrar@gwdg.de
Published
1999-04-01
Pages
1-10
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1220120
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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