ArticleBiophysical journal2017
Allosteric Control of a Plant Receptor Kinase through S-Glutathionylation.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 48 citations in OpenAlex.
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- Robust AMBER Force Field Parameters for Glutathionylated Cysteines.International journal of molecular sciences · 2023Article
- Effect of histidine covalent modification on strigolactone receptor activation and selectivity.Biophysical journal · 2023Article
- Thirty years of molecular dynamics simulations on posttranslational modifications of proteins.Physical chemistry chemical physics : PCCP · 2022Review
- Glutathione Metabolism in Plants under Stress: Beyond Reactive Oxygen Species Detoxification.Metabolites · 2021Review
- Role of Position K+4 in the Phosphorylation and Dephosphorylation Reaction Kinetics of the CheY Response Regulator.Biochemistry · 2021Article
- Cysteine modifications (oxPTM) and protein sulphenylation-mediated sulfenome expression in plants: evolutionary conserved signaling networks?Plant signaling & behavior · 2021Article
- Regulation of Three Key Kinases of Brassinosteroid Signaling Pathway.International journal of molecular sciences · 2020Review
- Article
- Structural Consequences of Multisite Phosphorylation in the BAK1 Kinase Domain.Biophysical journal · 2020Article
- Molecular Basis of the Glucose Transport Mechanism in Plants.ACS central science · 2019Article
- SAXS-guided Enhanced Unbiased Sampling for Structure Determination of Proteins and Complexes.Scientific reports · 2018Article
- Role of Computational Methods in Going beyond X-ray Crystallography to Explore Protein Structure and Dynamics.International journal of molecular sciences · 2018Review
- Oxidative stress in chronic lung disease: From mitochondrial dysfunction to dysregulated redox signaling.Molecular aspects of medicine · 2018Review
- Structural Basis for the Limited Response to Oxidative and Thiol-Conjugating Agents by Triosephosphate Isomerase From the Photosynthetic BacteriaFrontiers in molecular biosciences · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Growing evidence supports the importance of protein S-glutathionylation as a regulatory post-translational modification with functional consequences for proteins. Discoveries of redox-state-dependent protein kinase S-glutathionylation have fueled discussion of redox-sensitive signaling. Following previously published experimental evidence for S-glutathionylation induced deactivation of the Arabidopsis thaliana kinase BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED RECEPTOR-LIKE KINASE 1 (BAK1), we investigated the consequences of S-glutathionylation on the equilibrium conformational ensemble of BAK1 using all-atom molecular dynamics simulations. We found that glutathionylation of C408 allosterically destabilizes the active-like state of BAK1 and stabilizes an inactive conformation known to recur in protein kinases. Glutathionylation of C408 also has structural consequences throughout the BAK1 kinase domain, whereas glutathionylation of C353 in the N-lobe and C374 near the ATP-binding site have few notable effects on BAK1 compared with the unmodified protein. Our results suggest an allosteric mechanism for inhibition of BAK1 by C408 S-glutathionylation, and more generally, support the notion of protein kinase S-glutathionylation as a means of redox signaling in plant cells.
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