Interactions Between Protein Disulphide Isomerase and Peptides

Klappa, Peter; Hawkins, Hilary C.; Freedman, Robert B.

doi:10.1111/j.1432-1033.1997.t01-1-00037.x

Cited by 91 publications

(104 citation statements)

References 23 publications

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“…The binding affinity increases with increasing length of the substrate backbone, but for peptides of similar length, those containing Cys residues may bind 4-8-fold more strongly [94,95]. In contrast with earlier data [94], Klappa and co-workers [95] observed that hydrophobic interactions may determine the efficiency of binding.…”

Section: Peptide Bindingcontrasting

confidence: 61%

“…Peptide-binding studies using either somatostatin or a 28-residue peptide from the N-terminus of staphylococcal nuclease indicated that the interaction of peptides with PDI competes with the refolding of reduced, denatured RNase and scrambled RNase, reduces the efficiency of catalysis of insulin reduction, and inhibits the chaperone function of PDI in the refolding of denatured GAPDH [94][95][96]. This indicates not only that both peptide-and polypeptide-binding sites are the same or spatially juxtaposed, but also that they are close enough to the active site to inhibit redox activity when occupied by a polypeptide chain.…”

Section: Peptide Bindingmentioning

confidence: 99%

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

Ferrari

Söling

1999

Biochemical Journal

403

359

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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,

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Section: Peptide Bindingcontrasting

confidence: 61%

Section: Peptide Bindingmentioning

confidence: 99%

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

Ferrari

Söling

1999

Biochemical Journal

403

359

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“…The ER-luminal enzyme and chaperone PDI is the predominant binding partner in the ER lumen for glycosylation acceptor peptides and unglycosylated peptides irrespective of their thiol content (34)(35)(36). PDI is composed of four thioredoxin modules, two enzymatically active ones (a, aЈ) and two inactive ones (b, bЈ) (37).…”

Section: Release From Pdi Is Not Critical For Glycopeptide Export Fromentioning

confidence: 99%

The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane

Gillece

Pilon

Römisch

2000

Proc. Natl. Acad. Sci. U.S.A.

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Peptides and misfolded secretory proteins are transported efficiently from the endoplasmic reticulum (ER) lumen to the cytosol, where the proteins are degraded by proteasomes. Protein export depends on Sec61p, the ribosome-binding core component of the protein translocation channel in the ER membrane. We found that prebinding of ribosomes abolished export of a glycopeptide from yeast microsomes. Deletion of SSH1, which encodes a ribosomebinding Sec61p homologue in the ER, had no effect on glycopeptide export. A collection of cold-sensitive sec61 mutants displayed a variety of phenotypes: two mutants strongly defective in misfolded protein export from the ER, sec61-32 and sec61-41, displayed only minor peptide export defects. Glycopeptide export was severely impaired, however, in several sec61 mutants that were only marginally defective in misfolded protein export. In addition, a mutation in SEC63 strongly reduced peptide export from the ER. ER-luminal ATP was required for both misfolded protein and glycopeptide export. We conclude that the protein translocation channel in the ER membrane mediates glycopeptide transport across the ER membrane.

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“…Another important group of ER protein-folding enzymes is oxidoreductases that catalyze the formation of disulfide bonds. The best-known member of this group is protein disulfide isomerase (PDI), which recognizes unfolded hydrophobic amino acids on newly synthesized proteins (Freedman et al 2002;Klappa et al 1997). Following the docking with its substrates, PDI is able to oxidize reduced cysteines or isomerize pre-formed disulfide bonds through transient mixed disulfides with its CXXC active sites and substrates (Horibe et al 2004;Walker and Gilbert 1995).…”

Section: Introductionmentioning

confidence: 99%

Ero1α requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)

Gilady

Bui

Lynes

et al. 2010

Cell Stress and Chaperones

156

115

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Protein secretion from the endoplasmic reticulum (ER) requires the enzymatic activity of chaperones and oxidoreductases that fold polypeptides and form disulfide bonds within newly synthesized proteins. The best-characterized ER redox relay depends on the transfer of oxidizing equivalents from molecular oxygen through ER oxidoreductin 1 (Ero1) and protein disulfide isomerase to nascent polypeptides. The formation of disulfide bonds is, however, not the sole function of ER oxidoreductases, which are also important regulators of ER calcium homeostasis. Given the role of human Ero1α in the regulation of the calcium release by inositol 1,4,5-trisphosphate receptors during the onset of apoptosis, we hypothesized that Ero1α may have a redox-sensitive localization to specific domains of the ER. Our results show that within the ER, Ero1α is almost exclusively found on the mitochondria-associated membrane (MAM). The localization of Ero1α on the MAM is dependent on oxidizing conditions within the ER. Chemical reduction of the ER environment, but not ER stress in general leads to release of Ero1α from the MAM. In addition, the correct localization of Ero1α to the MAM also requires normoxic conditions, but not ongoing oxidative phosphorylation.

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Interactions Between Protein Disulphide Isomerase and Peptides

Cited by 91 publications

References 23 publications

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

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

The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane

Ero1α requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)

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