Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum

Soares Moretti, Ana Iochabel; Martins Laurindo, Francisco Rafael

doi:10.1016/j.abb.2016.11.007

Cited by 140Redox biology and oxidative stressEndoplasmic Reticulum Stress and DiseaseHeat shock proteins research

Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum

Soares Moretti, Ana Iochabel, Martins Laurindo, Francisco Rafael·2017·Archives of Biochemistry and Biophysics

DOI 10.1016/j.abb.2016.11.007

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Abstract

Protein disulfide isomerases are thiol oxidoreductase chaperones from thioredoxin superfamily. As redox folding catalysts from the endoplasmic reticulum (ER), their roles in ER-related redox homeostasis and signaling are well-studied. PDIA1 exerts thiol oxidation/reduction and isomerization, plus chaperone effects. Also, substantial evidence indicates that PDIs regulate thiol-disulfide switches in other cell locations such as cell surface and possibly cytosol. Subcellular PDI translocation routes remain unclear and seem Golgi-independent. The list of signaling and structural proteins reportedly regulated by PDIs keeps growing, via thiol switches involving oxidation, reduction and isomerization, S-(de)nytrosylation, (de)glutathyonylation and protein oligomerization. PDIA1 is required for agonist-triggered Nox NADPH oxidase activation and cell migration in vascular cells and macrophages, while PDIA1-dependent cytoskeletal regulation appears a converging pathway. Extracellularly, PDIs crucially regulate thiol redox signaling of thrombosis/platelet activation, e.g., integrins, and PDIA1 supports expansive caliber remodeling during injury repair via matrix/cytoskeletal organization. Some proteins display regulatory PDI-like motifs. PDI effects are orchestrated by expression levels or post-translational modifications. PDI is redox-sensitive, although probably not a mass-effect redox sensor due to kinetic constraints. Rather, the "all-in-one" organization of its peculiar redox/chaperone properties likely provide PDIs with precision and versatility in redox signaling, making them promising therapeutic targets.

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Reduced transcription of DnaJ heat shock protein family members and thioredoxin superfamily members further corroborates perturbed ER proteostasis in vEDS fibroblasts.
“In addition, the reduced transcription of members belonging to the DnaJ heat shock protein family, i.e., DNAJB7, DNAJB11, DNAJC3, DNAJC10, and DNAJC24, and to the thioredoxin superfamily, i.e., TXN, PDIA4, PDIA5, and PDIA6, which all act as intracellular mediators for correct protein folding and intracellular redox balance [105], further corroborates a perturbed ER proteostasis in vEDS fibroblasts”
From Cellular and Molecular Mechanisms in the Pathogenesis of Classical, Vascular, and Hypermobile Ehlers‒Danlos Syndromes (2019) · cites this paper as [105]
PDIA4, PDIA5, and PDIA6 are members of an expanding protein family known as protein disulfide isomerases that may also act as effectors of protein translocation of terminally un/misfolded proteins to the cytosol for their proteasomal degradation.
“Moreover, PDIA4, PDIA5, and PDIA6 are members of an expanding proteins family known as protein disulfide isomerases that may also act as effectors of protein translocation of terminally un/misfolded proteins to the cytosol for their proteasomal degradation [50].”
From Transcriptome analysis of skin fibroblasts with dominant negative COL3A1 mutations provides molecular insights into the etiopathology of vascular Ehlers-Danlos syndrome (2018) · cites this paper as [50]

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Authors: Soares Moretti, A. I., & Martins Laurindo, F. R.
Venue: Archives of Biochemistry and Biophysics
Publisher: Elsevier BV
Published: 2017-03
Volume: 617
Pages: 106-119
ISSN: 0003-9861 (ISSN-L)
DOI: 10.1016/j.abb.2016.11.007
OpenAlex: W2550575905
Cited by: 140
References: 200
Citations by year: 2026: 5 · 2025: 15 · 2024: 16 · 2023: 10 · 2022: 17 · 2021: 9 · 2020: 21 · 2019: 18 · 2018: 13 · 2017: 15 · 2016: 1
FWCI: 1.41
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Archives of Biochemistry and Biophysics (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: protein disulfide isomerase, PDIA1, thioredoxin superfamily, redox signaling, endoplasmic reticulum, molecular chaperones, S-nitrosylation, S-glutathionylation, protein oligomerization, NADPH oxidase activation, cell migration, thrombosis, platelet activation, integrins, cytoskeleton regulation, post-translational modification, therapeutic target
MeSH terms: Animals, Cytoskeleton, Cytosol, Disulfides, Endoplasmic Reticulum, Homeostasis, Humans, Kinetics, Oxidation-Reduction, Peroxides, Procollagen-Proline Dioxygenase, Protein Processing, Post-Translational, Signal Transduction, Molecular Chaperones, NADPH Oxidases, Protein Disulfide-Isomerases, Mice

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Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum

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