ArticleThe Journal of biological chemistry2012
Thioredoxin reductase linked to cytoskeleton by focal adhesion kinase reverses actin S-nitrosylation and restores neutrophil β(2) integrin function.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Selenium and Selenoproteins in Neutrophil Functions.Biological trace element research · 2026Review
- Thioredoxin system: mechanisms and therapeutic potential in mental disorders.Frontiers in pharmacology · 2026Review
- The Role of Thioredoxin System in Shank3 Mouse Model of Autism.Journal of molecular neuroscience : MN · 2024Article
- Nitric oxide (NO) modulates low temperature-stress signaling via S-nitrosation, a NO PTM, inducing ethylene biosynthesis inhibition leading to enhanced post-harvest shelf-life of agricultural produce.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023Review
- Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation.Molecules (Basel, Switzerland) · 2021Review
- The Role of Hyperbaric Oxygen Treatment for COVID-19: A Review.Advances in experimental medicine and biology · 2021Review
- Nitric Oxide and Electrophilic Cyclopentenone Prostaglandins in Redox signaling, Regulation of Cytoskeleton Dynamics and Intercellular Communication.Frontiers in cell and developmental biology · 2021Review
- Microparticle and interleukin-1β production with human simulated compressed air diving.Scientific reports · 2019Article
- Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling.Antioxidants & redox signaling · 2019Review
- Neutrophil microparticle production and inflammasome activation by hyperglycemia due to cytoskeletal instability.The Journal of biological chemistry · 2017Article
- Factors Associated with Nitric Oxide-mediated β2 Integrin Inhibition of Neutrophils.The Journal of biological chemistry · 2015Article
- The cysteine proteome.Free radical biology & medicine · 2015Review
- Antioxidant enzymes as redox-based biomarkers: a brief review.BMB reports · 2015Review
- A substrate trapping approach identifies proteins regulated by reversible S-nitrosylation.Molecular & cellular proteomics : MCP · 2014Article
- Neutrophils generate microparticles during exposure to inert gases due to cytoskeletal oxidative stress.The Journal of biological chemistry · 2014Article
- Shear-induced endothelial mechanotransduction: the interplay between reactive oxygen species (ROS) and nitric oxide (NO) and the pathophysiological implications.Journal of biomedical science · 2014Review
- Actin cytoskeleton redox proteome oxidation by cadmium.American journal of physiology. Lung cellular and molecular physiology · 2013Article
- Selective targeting of the cysteine proteome by thioredoxin and glutathione redox systems.Molecular & cellular proteomics : MCP · 2013Article
- The redox proteome.The Journal of biological chemistry · 2013Review
- Nitric-oxide synthase-2 linkage to focal adhesion kinase in neutrophils influences enzyme activity and β2 integrin function.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The investigation goal was to identify mechanisms for reversal of actin S-nitrosylation in neutrophils after exposure to high oxygen partial pressures. Prior work has shown that hyperoxia causes S-nitrosylated actin (SNO-actin) formation, which mediates β(2) integrin dysfunction, and these changes can be reversed by formylmethionylleucylphenylalanine or 8-bromo-cyclic GMP. Herein we show that thioredoxin reductase (TrxR) is responsible for actin denitrosylation. Approximately 80% of cellular TrxR is localized to the cytosol, divided between the G-actin and short filamentous actin (sF-actin) fractions based on Triton solubility of cell lysates. TrxR linkage to sF-actin requires focal adhesion kinase (FAK) based on immunoprecipitation studies. S-Nitrosylation accelerates actin filament turnover (by mechanisms described previously (Thom, S. R., Bhopale, V. M., Yang, M., Bogush, M., Huang, S., and Milovanova, T. (2011) Neutrophil β(2) integrin inhibition by enhanced interactions of vasodilator stimulated phosphoprotein with S-nitrosylated actin. J. Biol. Chem. 286, 32854-32865), which causes FAK to disassociate from sF-actin. TrxR subsequently dissociates from FAK, and the physical separation from actin impedes denitrosylation. If SNO-actin is photochemically reduced with UV light or if actin filament turnover is impeded by incubations with cytochalasin D, latrunculin B, 8-bromo-cGMP, or formylmethionylleucylphenylalanine, FAK and TrxR reassociate with sF-actin and cause SNO-actin removal. FAK-TrxR association can also be demonstrated using isolated enzymes in ex vivo preparations. Uniquely, the FAK kinase domain is the site of TrxR linkage. We conclude that through its scaffold function, FAK influences TrxR activity and actin S-nitrosylation.
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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.