ArticleInternational journal of cell biology2012
S-Glutathionylation of Protein Disulfide Isomerase Regulates Estrogen Receptor α Stability and Function.
Article in International journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.Biochemistry · 2026Review
- Exploring the Role of Unconventional Post-Translational Modifications in Cancer Diagnostics and Therapy.Current protein & peptide science · 2024Review
- Protein disulfide isomerase family mediated redox regulation in cancer.Advances in cancer research · 2023Review
- Redox stress in COVID-19: Implications for hematologic disorders.Best practice & research. Clinical haematology · 2022Review
- Pdia4 regulates β-cell pathogenesis in diabetes: molecular mechanism and targeted therapy.EMBO molecular medicine · 2021Article
- GlutathioneThe Journal of pharmacology and experimental therapeutics · 2021Article
- Polymorphisms in Genes Encoding Glutathione Transferase Pi and Glutathione Transferase Omega Influence Prostate Cancer Risk and Prognosis.Frontiers in molecular biosciences · 2021Article
- PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly.Molecules (Basel, Switzerland) · 2020Review
- Article
- An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation.Free radical biology & medicine · 2018Review
- Succination of Protein Disulfide Isomerase Links Mitochondrial Stress and Endoplasmic Reticulum Stress in the Adipocyte During Diabetes.Antioxidants & redox signaling · 2017Article
- Protein disulfide isomerase a4 acts as a novel regulator of cancer growth through the procaspase pathway.Oncogene · 2017Article
- Stress-Induced Protein S-Glutathionylation and S-Trypanothionylation in African Trypanosomes-A Quantitative Redox Proteome and Thiol Analysis.Antioxidants & redox signaling · 2017Article
- Glutathione S-Transferase P-Mediated Protein S-Glutathionylation of Resident Endoplasmic Reticulum Proteins Influences Sensitivity to Drug-Induced Unfolded Protein Response.Antioxidants & redox signaling · 2017Article
- Formation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative Stress.The Journal of biological chemistry · 2016Article
- Paradoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health Implications.Physiological reviews · 2016Review
- Redox theory of aging.Redox biology · 2015Review
- The cysteine proteome.Free radical biology & medicine · 2015Review
- Novel roles for protein disulphide isomerase in disease states: a double edged sword?Frontiers in cell and developmental biology · 2015Review
- EF24 prevents rotenone-induced estrogenic status alteration in breast cancer.Cell biology international · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
S-Glutathionylation of cysteine residues within target proteins is a posttranslational modification that alters structure and function. We have shown that S-glutathionylation of protein disulfide isomerase (PDI) disrupts protein folding and leads to the activation of the unfolded protein response (UPR). PDI is a molecular chaperone for estrogen receptor alpha (ERα). Our present data show in breast cancer cells that S-glutathionylation of PDI interferes with its chaperone activity and abolishes its capacity to form a complex with ERα. Such drug treatment also reverses estradiol-induced upregulation of c-Myc, cyclinD1, and P21(Cip), gene products involved in cell proliferation. Expression of an S-glutathionylation refractory PDI mutant diminishes the toxic effects of PABA/NO. Thus, redox regulation of PDI causes its S-glutathionylation, thereby mediating cell death through activation of the UPR and abrogation of ERα stability and signaling.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.