ArticleArchives of biochemistry and biophysics2014
Hypothiocyanous acid oxidation of tubulin cysteines inhibits microtubule polymerization.
Article in Archives of biochemistry and biophysics, 2014. 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, 30 citations in OpenAlex.
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- Nrf1 acts as a highly-conserved determinon for maintaining robust redox homeostasis in the eco-evo-devo process of life histories.Cell stress · 2025Review
- Hypothiocyanous Acid Disrupts the Barrier Function of Brain Endothelial Cells.Antioxidants (Basel, Switzerland) · 2022Article
- Oxidative stress pathogenically remodels the cardiac myocyte cytoskeleton via structural alterations to the microtubule lattice.Developmental cell · 2021Article
- Mitochondrial Reactive Oxygen Species (ROS) Production Alters Sperm Quality.Antioxidants (Basel, Switzerland) · 2021Review
- Xanthatin inhibits STAT3 and NF-κB signalling by covalently binding to JAK and IKK kinases.Journal of cellular and molecular medicine · 2019Article
- NADPH oxidase mediates microtubule alterations and diaphragm dysfunction in dystrophic mice.eLife · 2018Article
- Article
- The role of Nox-mediated oxidation in the regulation of cytoskeletal dynamics.Current pharmaceutical design · 2015Review
- The pro-oxidant buthionine sulfoximine (BSO) reduces tumor growth of implanted Lewis lung carcinoma in mice associated with increased protein carbonyl, tubulin abundance, and aminopeptidase activity.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Article
- The interplay between ROS and tubulin cytoskeleton in plants.Plant signaling & behavior · 2014Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Thiol oxidation is a probable outcome of cellular oxidative stress and is linked to degenerative disease progression. In addition, protein thiol redox reactions are increasingly identified as a mechanism to regulate protein structure and function. We assessed the effect of hypothiocyanous acid on the cytoskeletal protein tubulin. Total cysteine oxidation by hypothiocyanous and hypochlorous acids was monitored by labeling tubulin with 5-iodoacetamidofluorescein and by detecting higher molecular weight inter-chain tubulin disulfides by Western blot under nonreducing conditions. Hypothiocyanous acid induced nearly stoichiometric oxidation of tubulin cysteines (1.9 mol cysteine/mol oxidant) and no methionine oxidation was observed. Because disulfide reducing agents restored all the polymerization activity that was lost due to oxidant treatment, we conclude that cysteine oxidation of tubulin inhibits microtubule polymerization. Hypothiocyanous acid oxidation of tubulin cysteines was markedly decreased in the presence of 4% glycerol, a component of the tubulin purification buffer. Due to its instability and buffer- and pH-dependent reactivity, hypothiocyanous acid studies require careful consideration of reaction conditions.
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