ArticleProceedings of the National Academy of Sciences of the United States of America2013
Selective activation of oxidized PTP1B by the thioredoxin system modulates PDGF-β receptor tyrosine kinase signaling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 97 citations in OpenAlex.
- Context‑dependent targeting of thioredoxin reductase 1 in cancer: a mechanistic review.Magyar onkologia · 2026Review
- Intracellular enzymatic reducing systems control receptor tyrosine kinase signaling via PTP1B.Science advances · 2026Article
- Mechanisms, functions and therapeutic targeting of protein tyrosine phosphatases.Nature reviews. Molecular cell biology · 2026Review
- Beyond Antioxidants: How Redox Pathways Shape Cellular Signaling and Disease Outcomes.Antioxidants (Basel, Switzerland) · 2025Review
- Fenvalerate exposure induces AKT/AMPK-dependent alterations in glucose metabolism in hepatoma cells.Frontiers in pharmacology · 2025Article
- Reactive oxygen species: Janus-faced molecules in the era of modern cancer therapy.Journal for immunotherapy of cancer · 2024Review
- Functional and clinical roles of stromal PDGF receptors in tumor biology.Cancer metastasis reviews · 2024Review
- TRP14 is the rate-limiting enzyme for intracellular cystine reduction and regulates proteome cysteinylation.The EMBO journal · 2024Article
- Protein tyrosine phosphatase 1B in metabolic diseases and drug development.Nature reviews. Endocrinology · 2024Review
- Measuring the Reversible Oxidation of Protein Tyrosine Phosphatases Using a Modified Cysteinyl-Labeling Assay.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Reactive oxygen species and its role in pathogenesis and resistance to therapy in acute myeloid leukemia.Cancer drug resistance (Alhambra, Calif.) · 2024Review
- Protein Tyrosine Phosphatase regulation by Reactive Oxygen Species.Advances in cancer research · 2024Review
- HInternational journal of molecular sciences · 2023Article
- Editorial: Small molecule inhibitors targeting mammalian selenoprotein thioredoxin reductases (TXNRDs): Interactions, mechanisms, and applications.Frontiers in molecular biosciences · 2023Article
- Interplay of carbon dioxide and peroxide metabolism in mammalian cells.The Journal of biological chemistry · 2022Review
- Redox regulation of PTPN22 affects the severity of T-cell-dependent autoimmune inflammation.eLife · 2022Article
- Oxidative stress promotes fibrosis in systemic sclerosis through stabilization of a kinase-phosphatase complex.JCI insight · 2022Article
- A Comprehensive Review on Selenium and Its Effects on Human Health and Distribution in Middle Eastern Countries.Biological trace element research · 2022Review
- Redox regulation of the insulin signalling pathway.Redox biology · 2021Review
- Qualitative Differences in Protection of PTP1B Activity by the Reductive Trx1 or TRP14 Enzyme Systems upon Oxidative Challenges with Polysulfides or HAntioxidants (Basel, Switzerland) · 2021Article
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Authors and funding
12 authors at 6 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inhibitory reversible oxidation of protein tyrosine phosphatases (PTPs) is an important regulatory mechanism in growth factor signaling. Studies on PTP oxidation have focused on pathways that increase or decrease reactive oxygen species levels and thereby affect PTP oxidation. The processes involved in reactivation of oxidized PTPs remain largely unknown. Here the role of the thioredoxin (Trx) system in reactivation of oxidized PTPs was analyzed using a combination of in vitro and cell-based assays. Cells lacking the major Trx reductase TrxR1 (Txnrd1(-/-)) displayed increased oxidation of PTP1B, whereas SHP2 oxidation was unchanged. Furthermore, in vivo-oxidized PTP1B was reduced by exogenously added Trx system components, whereas SHP2 oxidation remained unchanged. Trx1 reduced oxidized PTP1B in vitro but failed to reactivate oxidized SHP2. Interestingly, the alternative TrxR1 substrate TRP14 also reactivated oxidized PTP1B, but not SHP2. Txnrd1-depleted cells displayed increased phosphorylation of PDGF-β receptor, and an enhanced mitogenic response, after PDGF-BB stimulation. The TrxR inhibitor auranofin also increased PDGF-β receptor phosphorylation. This effect was not observed in cells specifically lacking PTP1B. Together these results demonstrate that the Trx system, including both Trx1 and TRP14, impacts differentially on the oxidation of individual PTPs, with a preference of PTP1B over SHP2 activation. The studies demonstrate a previously unrecognized pathway for selective redox-regulated control of receptor tyrosine kinase signaling.
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