ArticleThe FEBS journal2020
Vimentin S-glutathionylation at Cys328 inhibits filament elongation and induces severing of mature filaments in vitro.
Article in The FEBS journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- Type III intermediate filaments as novel CoAlation targets.Redox report : communications in free radical research · 2026Article
- Vimentin remodeling in response to oxidants and electrophiles is modulated by pH.Science advances · 2026Article
- Alexander disease mutations differentially sensitize glial fibrillary acidic protein (GFAP) to posttranslational modifications and network disruption by oxidants.Redox biology · 2026Article
- Intermediate Filaments: Structure-Mechanics Crosstalk.Sub-cellular biochemistry · 2026Review
- Linking Cell Architecture to Mitochondrial Signaling in Neurodegeneration: The Role of Intermediate Filaments.International journal of molecular sciences · 2025Review
- Hypoxia-Induced PRMT1 Lactylation Drives Vimentin Arginine Asymmetric Dimethylation in Tumor Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Continuous self-repair protects vimentin intermediate filaments from fragmentation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure and function of vimentin in the generation and secretion of extracellular vimentin in response to inflammation.Cell communication and signaling : CCS · 2025Review
- From Cell Architecture to Mitochondrial Signaling: Role of Intermediate Filaments in Health, Aging, and Disease.International journal of molecular sciences · 2025Review
- Oxidative stress elicits the remodeling of vimentin filaments into biomolecular condensates.Redox biology · 2024Article
- Article
- Type III intermediate filaments in redox interplay: key role of the conserved cysteine residue.Biochemical Society transactions · 2024Review
- Article
- Emerging chemistry and biology in protein glutathionylation.Current opinion in chemical biology · 2022Review
- Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.Antioxidants (Basel, Switzerland) · 2022Review
- Intracellular Protein S-Nitrosylation-A Cells Response to Extracellular S100B and RAGE Receptor.Biomolecules · 2022Article
- Super-sensitive bifunctional nanoprobe: Self-assembly of peptide-driven nanoparticles demonstrating tumor fluorescence imaging and therapy.Acta pharmaceutica Sinica. B · 2022Article
- Impact of Vimentin on Regulation of Cell Signaling and Matrix Remodeling.Frontiers in cell and developmental biology · 2022Review
- The role of cysteine residues in the allosteric modulation of the chromophore phototransformations of biphotochromic fluorescent protein SAASoti.Scientific reports · 2021Article
- Glutathione S-Transferases in Cancer.Antioxidants (Basel, Switzerland) · 2021Review
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vimentin intermediate filaments are a significant component of the cytoskeleton in cells of mesenchymal origin. In vivo, filaments assemble and disassemble and thus participate in the dynamic processes of the cell. Post-translational modifications (PTMs) such as protein phosphorylation regulate the multiphasic association of vimentin from soluble complexes to insoluble filaments and the reverse processes. The thiol side chain of the single vimentin cysteine at position 328 (Cys328) is a direct target of oxidative modifications inside cells. Here, we used atomic force microscopy, electron microscopy and a novel hydrogen-deuterium exchange mass spectrometry (HDex-MS) procedure to investigate the structural consequences of S-nitrosylation and S-glutathionylation of Cys328 for in vitro oligomerisation of human vimentin. Neither modification affects the lateral association of tetramers to unit-length filaments (ULF). However, S-glutathionylation of Cys328 blocks the longitudinal assembly of ULF into extended filaments. S-nitrosylation of Cys328 does not hinder but slows down the elongation. Likewise, S-glutathionylation of preformed vimentin filaments causes their extensive fragmentation to smaller oligomeric species. Chemical reduction of the S-glutathionylated Cys328 thiols induces reassembly of the small fragments into extended filaments. In conclusion, our in vitro results suggest S-glutathionylation as a candidate PTM for an efficient molecular switch in the dynamic rearrangements of vimentin intermediate filaments, observed in vivo, in response to changes in cellular redox status. Finally, we demonstrate that HDex-MS is a powerful method for probing the kinetics of vimentin filament formation and filament disassembly induced by PTMs.
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