Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation

Wolhuter, Kathryn; Whitwell, Harry J.; Switzer, Christopher H.; Burgoyne, Joseph R.; Timms, John F.; Eaton, Philip

doi:10.1016/j.molcel.2017.12.019

Cited by 111Redox biology and oxidative stressNitric Oxide and Endothelin EffectsSulfur Compounds in Biology

Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation

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Wolhuter, Kathryn, Whitwell, Harry J., Switzer, Christopher H., Burgoyne, Joseph R., Timms, John F., Eaton, Philip·2018·Molecular Cell

DOI 10.1016/j.molcel.2017.12.019PMC PMC5807093

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Abstract

S-nitrosation, commonly referred to as S-nitrosylation, is widely regarded as a ubiquitous, stable post-translational modification that directly regulates many proteins. Such a widespread role would appear to be incompatible with the inherent lability of the S-nitroso bond, especially its propensity to rapidly react with thiols to generate disulfide bonds. As anticipated, we observed robust and widespread protein S-nitrosation after exposing cells to nitrosocysteine or lipopolysaccharide. Proteins detected using the ascorbate-dependent biotin switch method are typically interpreted to be directly regulated by S-nitrosation. However, these S-nitrosated proteins are shown to predominantly comprise transient intermediates leading to disulfide bond formation. These disulfides are likely to be the dominant end effectors resulting from elevations in nitrosating cellular nitric oxide species. We propose that S-nitrosation primarily serves as a transient intermediate leading to disulfide formation. Overall, we conclude that the current widely held perception that stable S-nitrosation directly regulates the function of many proteins is significantly incorrect.

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MPO is found predominantly in neutrophils and monocytes and catalyzes the reaction of hydrogen peroxide to produce several reactive species, mainly hypochlorous acid (HOCl).
“MPO is found predominantly in neutrophils and monocytes and catalyzes the reaction of hydrogen peroxide to produce several reactive species, mainly hypochlorous acid (HOCl) (discussed in sect. IVB) (516, 1021).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1021]
HOCl plays a major role in the microbicidal actions of neutrophils.
“This highly reactive oxidizing and chlorinating agent plays a major role in the microbicidal actions of neutrophils (15, 1021).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1021]

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S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
Jia, L., Bonaventura, C., Bonaventura, J., & Stamler, J. S. (1996) · Nature · doi:10.1038/380221a0 · Cited by 1,586 · see citing works
Reversible Inactivation of the Tumor Suppressor PTEN by H2O2
Lee, S.-R., Yang, K., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,061 · see citing works
(S)NO Signals: Translocation, Regulation, and a Consensus Motif
Stamler, J. S., Toone, E. J., Lipton, S. A., & Sucher, N. J. (1997) · Neuron · doi:10.1016/s0896-6273(00)80310-4 · Cited by 674 · see citing works
“NONOates” (1-substituted diazen-1-ium-1,2-diolates) as nitric oxide donors: Convenient nitric oxide dosage forms
Keefer, L. K., Nims, R. W., Davies, K. M., & Wink, D. A. (1996) · Methods in Enzymology · doi:10.1016/s0076-6879(96)68030-6 · Cited by 670 · see citing works
NO+, NO, and NO- donation by S-nitrosothiols-implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation
Arnelle, D. R., & Stamler, J. S. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1231 · Cited by 604 · cited 1× · see citing works
“S-nitrosated thiols are intrinsically unstable, especially in the intracellular context, where they react with reduced metal ions as well as abundant thiols to generate disulfides (Arnelle and Stamler, 1995).”
Protein denitrosylation: enzymatic mechanisms and cellular functions
Benhar, M., Forrester, M. T., & Stamler, J. S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2764 · Cited by 519 · see citing works
Regulation by S-Nitrosylation of Protein Post-translational Modification
Hess, D. T., & Stamler, J. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.285742 · Cited by 385 · see citing works
S-Nitrosylation of mitochondrial caspases
Mannick, J. B., Schonhoff, C. M., Papeta, N., Ghafourifar, P., Szibor, M., Fang, K., & Gaston, B. M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104008 · Cited by 363 · see citing works
The Endothelial Nitric-oxide Synthase-Caveolin Regulatory Cycle
Féron, O., Saldaña, F., Michel, J. B., & Michel, T. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3125 · Cited by 361 · see citing works
Nitrosative Stress: Activation of the Transcription Factor OxyR
Hausladen, A., Privalle, C. T., Keng, T., DeAngelo, J., & Stamler, J. S. (1996) · Cell · doi:10.1016/s0092-8674(00)80147-6 · Cited by 359 · see citing works
The chemistry of the S -nitrosoglutathione/glutathione system
Singh, S. P., Wishnok, J. S., Keshive, M., Deen, W. M., & Tannenbaum, S. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14428 · Cited by 336 · see citing works
Neuronal growth cone collapse and inhibition of protein fatty acylation by nitric oxide
Hess, D. T., Patterson, S. I., Smith, D. S., & Skene, J. H. P. (1993) · Nature · doi:10.1038/366562a0 · Cited by 327 · see citing works
Nitric oxide's reactions with hemoglobin: a view through the SNO-storm
Gladwin, M. T., Lancaster, J. R., Freeman, B. Α., & Schechter, A. N. (2003) · Nature Medicine · doi:10.1038/nm0503-496 · Cited by 288 · see citing works
S -nitrosylation of dimethylarginine dimethylaminohydrolase regulates enzyme activity: Further interactions between nitric oxide synthase and dimethylarginine dimethylaminohydrolase
LEIPER, J. M., Murray‐Rust, J., McDonald, N. Q., & Vallance, P. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212269799 · Cited by 288 · see citing works
Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path
Lee, C., Lee, S. M., Mukhopadhyay, P., Kim, S. J., Lee, S. C., Ahn, W.-S., Yu, M., Storz, G., & Ryu, S. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb856 · Cited by 281 · see citing works
Coronary Hemodynamics in Endothelial NO Synthase Knockout Mice
Gödecke, A., Decking, U. K. M., Ding, Z., Hirchenhain, J., Bidmon, H. J., Gödecke, S., & Schrader, J. (1998) · Circulation Research · doi:10.1161/01.res.82.2.186 · Cited by 263 · see citing works
The chemical biology of S-nitrosothiols
Broniowska, K. A., & Hogg, N. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4590 · Cited by 259 · see citing works
Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide
Bosworth, C. A., Toledo, J. C., Zmijewski, J. W., Li, Q., & Lancaster, J. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710416106 · Cited by 220 · see citing works
On–off system for PI3-kinase–Akt signaling through S -nitrosylation of phosphatase with sequence homology to tensin (PTEN)
Numajiri, N., Takasawa, K., Nishiya, T., Tanaka, H., Ohno, K., Hayakawa, W., Asada, M., Matsuda, H., Azumi, K., Kamata, H., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103503108 · Cited by 174 · see citing works
Nitrosothiol Reactivity Profiling Identifies S-Nitrosylated Proteins with Unexpected Stability
Paige, J. S., Xu, G., Stancevic, B., & Jaffrey, S. R. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.10.013 · Cited by 173 · see citing works
Oxidation of Cofilin Mediates T Cell Hyporesponsiveness under Oxidative Stress Conditions
Klemke, M., Wabnitz, G. H., Funke, F., Funk, B., Kirchgessner, H., & Samstag, Y. (2008) · Immunity · doi:10.1016/j.immuni.2008.06.016 · Cited by 162 · see citing works
S-Nitrosohemoglobin Is Unstable in the Reductive Erythrocyte Environment and Lacks O2/NO-linked Allosteric Function
Gladwin, M. T., Wang, X., Reiter, C. D., Yang, B. K., Vivas, E. X., Bonaventura, C., & Schechter, A. N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203236200 · Cited by 160 · see citing works
Neuronal Nitric Oxide Synthase Protects Against Myocardial Infarction-Induced Ventricular Arrhythmia and Mortality in Mice
Burger, D. E., Lu, X., Lei, M., Xiang, F.-L., Hammoud, L., Jiang, M., Wang, H., Jones, D. L., Sims, S. M., & Feng, Q. (2009) · Circulation · doi:10.1161/circulationaha.108.846402 · Cited by 124 · see citing works
Protein S-glutathiolation: Redox-sensitive regulation of protein function
Hill, B., & Bhatnagar, A. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.07.009 · Cited by 122 · see citing works
Thiyl radicals react with nitric oxide to form S-nitrosothiols with rate constants near the diffusion-controlled limit
Madej, E., Folkes, L. K., Wardman, P., Czapski, G., & Goldstein, S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.02.015 · Cited by 105 · see citing works
Kinetic Analysis of Intracellular Concentrations of Reactive Nitrogen Species
Lim, C. H., Dedon, P. C., & Deen, W. M. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800213b · Cited by 93 · see citing works
Nitro-fatty acid inhibition of neointima formation after endoluminal vessel injury
Cole, M. P., Rudolph, T. K., Khoo, N. K. H., Motanya, U. N., Golin-Bisello, F., Wertz, J. W., Schopfer, F. J., Rudolph, V., Woodcock, S. R., Bolisetty, S., et al. (2009) · Circulation Research · doi:10.1161/circresaha.109.199075 · Cited by 69 · see citing works
Mechanisms Underlying Activation of Soluble Guanylate Cyclase by the Nitroxyl Donor Angeli’s Salt
Zeller, A., Wenzl, M. V., Beretta, M., Stessel, H., Russwurm, M., Koesling, D., Schmidt, K., & Mayer, B. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.059915 · Cited by 65 · see citing works
Neuronal Nitric Oxide Synthase-Dependent S-Nitrosylation of Gephyrin Regulates Gephyrin Clustering at GABAergic Synapses
Dejanovic, B., & Schwarz, G. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0531-14.2014 · Cited by 62 · see citing works
Effect of protein S-nitrosylation on autolysis and catalytic ability of μ-calpain
Liu, R., Li, Y., Wang, M., Zhou, G., & Zhang, W. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.06.104 · Cited by 59 · see citing works
Protein kinase G oxidation is a major cause of injury during sepsis
Rudyk, O., Phinikaridou, A., Prysyazhna, O. D., Burgoyne, J. R., Botnar, R. M., & Eaton, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301026110 · Cited by 54 · see citing works
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Shoman, M. E., DuMond, J. F., Isbell, T. S., Crawford, J. H., Brandon, A. P., Honovar, J., Vitturi, D. A., White, C. R., Patel, R. P., & King, S. B. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm101432z · Cited by 54 · see citing works
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Hamer, M., Suárez, S., Neuman, N. I., Álvarez, L., Muñoz, M., Marti, M. A., & Doctorovich, F. A. (2015) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5b01347 · Cited by 40 · see citing works
Proteomic Profiling of Nitrosative Stress: Protein S- Oxidation Accompanies S- Nitrosylation
Wang, Y.-T., Piyankarage, S. C., Williams, D. L., & Thatcher, G. R. J. (2014) · ACS Chemical Biology · doi:10.1021/cb400547u · Cited by 33 · see citing works
S‐nitrosylation of Cofilin‐1 Serves as a Novel Pathway for VEGF‐Stimulated Endothelial Cell Migration
Zhang, H., Wang, W., Feng, L., Yang, Y., Zheng, J. J., Huang, L., & Chen, D. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24724 · Cited by 31 · see citing works

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Corpas, F. J., González‐Gordo, S., Rodríguez-Ruiz, M., MU袿Z-VARGAS, M. A., & PALMA, J. (2021) · Biocell · doi:10.32604/biocell.2021.017300 · Cited by 17 · see citing works
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Köhler, I. (2024) · Linköping University medical dissertations · doi:10.3384/9789180758390 · Cited by 1 · see citing works
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Papaleo, E., Tiberti, M., Arnaudi, M., Pecorari, C., Faienza, F., Cantwell, L., Degn, K., Pacello, F., Battistoni, A., Lambrughi, M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.11.519943

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Self-citation
Evidence against stable protein S-nitrosylation as a widespread mechanism of post-translational regulation. Wolhuter et al
Eaton, P. (2018) · Data Archiving and Networked Services (DANS) · doi:10.17632/k2t8nx8kh5.1
Self-citation
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Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153 · see citing works

Authors: Wolhuter, K., Whitwell, H. J., Switzer, C. H., Burgoyne, J. R., Timms, J. F., & Eaton, P.
Affiliations: St Thomas' Hospital (GB)
University College London (GB)
Corresponding author: Eaton, Philip
ORCID: Wolhuter, Kathryn
Whitwell, Harry J.
Switzer, Christopher H.
Burgoyne, Joseph R.
Timms, John F.
Eaton, Philip
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2018-02
Volume: 69
Issue: 3
Pages: 438-450.e5
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2017.12.019
PMC: PMC5807093
OpenAlex: W2784924795
Cited by: 111
References: 35
Citations by year: 2026: 8 · 2025: 13 · 2024: 9 · 2023: 10 · 2022: 8 · 2021: 21 · 2020: 18 · 2019: 10 · 2018: 14
FWCI: 5.60
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Molecular Cell (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
Research Portal (King's College London) (submittedVersion, cc-by)
Queen Mary Research Online (Queen Mary University of London) (submittedVersion, cc-by)
Spiral (Imperial College London) (submittedVersion, cc-by)
Funders: British Heart Foundation (BHF RG/12/12/29872)
Department of Health and Social Care
Medical Research Council (MR/L009684/1)
European Research Council (339095)
Guy's and St Thomas' NHS Foundation Trust
University College London Hospitals NHS Foundation Trust
National Institute for Health and Care Research
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
Keywords: S-nitrosylation, post-translational modification, nitric oxide, disulfide bond formation, lipopolysaccharide, transient intermediates, protein regulation
MeSH terms: Cysteine, Disulfides, Humans, Nitric Oxide, Oxidation-Reduction, Protein Processing, Post-Translational, Proteins, Sulfhydryl Compounds, Nitrosation, S-Nitrosothiols, Proteomics, Proteolysis

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Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation

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