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Type III intermediate filaments as novel CoAlation targets.

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Title: Type III intermediate filaments as novel CoAlation targets.
Authors: Goya-Iglesias N; Department of Molecular and Cellular Biosciences, Centro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain., Yu BYK; Department of Structural and Molecular Biology, University College London, London, UK., Gout I; Department of Structural and Molecular Biology, University College London, London, UK.; Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv, Ukraine., Pérez-Sala D; Department of Molecular and Cellular Biosciences, Centro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain.
Source: Redox report : communications in free radical research [Redox Rep] 2026 Dec 31; Vol. 31 (1), pp. 2692797. Date of Electronic Publication: 2026 Jun 24.
Publication Type: Journal Article
Language: English
Journal Info: Publisher: Taylor & Francis Country of Publication: England NLM ID: 9511366 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1743-2928 (Electronic) Linking ISSN: 13510002 NLM ISO Abbreviation: Redox Rep Subsets: MEDLINE
Imprint Name(s): Publication: 2016- : Abingdon : Taylor & Francis
Original Publication: Edinburgh ; New York : Churchill Livingstone, c1994-
MeSH Terms: Vimentin*/metabolism , Intermediate Filaments*/metabolism , Desmin*/metabolism , Glial Fibrillary Acidic Protein*/metabolism, Cysteine/metabolism ; Humans ; Animals ; Protein Processing, Post-Translational ; Oxidative Stress ; Oxidation-Reduction
Abstract: Objectives: Type III intermediate filaments, such as vimentin, GFAP, and desmin, are involved in cell mechanics, signaling, and stress responses, and are tightly regulated by posttranslational modifications (PTMs). The monomers of these proteins possess a single cysteine residue that plays a key role in network remodeling under oxidative stress. CoAlation is a PTM involving mixed disulfide bond formation between a protein thiol and the coenzyme A (CoA) thiol. Here we aim to investigate the potential CoAlation of vimentin, GFAP, and desmin, and its functional consequences.
Methods: CoAlation of type III intermediate filaments and its interplay with other oxidative modifications was assessed in vitro by gel assays and immunological detection, whereas its effect on vimentin filament assembly was evaluated by electron microscopy. In cells, CoAlation was evaluated by CoA immunofluorescence, proximity ligation assay, and/or immunoprecipitation.
Results: CoAlation of vimentin, GFAP, and desmin occurs in vitro and in cells, and is enhanced by oxidants. In the case of vimentin, CoA reciprocally influences other thiol group modifications in vitro, attenuating disulfide-mediated oligomerization and cysteine alkylation. Moreover, in vitro polymerization in the presence of CoA results in shorter vimentin filaments.
Conclusion: We show that vimentin, GFAP, and desmin are CoAlated at their single cysteine residues. Our results suggest that CoAlation may influence filament assembly and compete with other cysteine modifications. Moreover, given its reversibility, CoAlation could potentially play a protective role against more deleterious modifications, such as irreversible cysteine oxidation.
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Contributed Indexing: Keywords: CoA; CoAlation; desmin; glial fibrillary acidic protein (GFAP); intermediate filaments; posttranslational modifications (PTMs); protein cysteine oxidation; vimentin
Substance Nomenclature: 0 (Vimentin)
0 (Desmin)
0 (Glial Fibrillary Acidic Protein)
K848JZ4886 (Cysteine)
Entry Date(s): Date Created: 20260625 Date Completed: 20260625 Latest Revision: 20260813
Update Code: 20260814
PubMed Central ID: PMC13307387
DOI: 10.1080/13510002.2026.2692797
PMID: 42343562
Database: MEDLINE
Description
ISSN:1743-2928
DOI:10.1080/13510002.2026.2692797