ArticleProtein & cell2014
DSSylation, a novel protein modification targets proteins induced by oxidative stress, and facilitates their degradation in cells.
Article in Protein & cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 12 citations in OpenAlex.
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- Heat Shock Protein 90: From Molecular Chaperone Function to Therapeutic Targeting in Malignancies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Exploring the intersection between necromass reutilization and genome protection reveals novel proteins that contribute to both processes in Ustilago maydis.Biology direct · 2026Article
- The Arabidopsis Mutant of the Small Intrinsically Disordered Protein DSS1(V) Exhibits Increased Sensitivity to Drought Stress.Plant direct · 2026Article
- DSS1 inhibits autophagy to activate epithelial-mesenchymal transition in a pro-metastatic niche of renal cell carcinoma.Nature communications · 2025Article
- DNA-PKcs as an upstream mediator of OCT4-induced MYC activation in small cell lung cancer.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Article
- CRISPR/Cas9-Targeted Disruption of Two Highly HomologousInternational journal of molecular sciences · 2023Article
- Intrinsically disordered protein AtDSS1(V) participates in plant defense response to oxidative stress.Protoplasma · 2021Article
- Development of cell-based high throughput luminescence assay for drug discovery in inhibiting OCT4/DNA-PKcs and OCT4-MK2 interactions.Biotechnology and bioengineering · 2021Article
- MYC transcription activation mediated by OCT4 as a mechanism of resistance to 13-cisRA-mediated differentiation in neuroblastoma.Cell death & disease · 2020Article
- Ceramide synthase-6 confers resistance to chemotherapy by binding to CD95/Fas in T-cell acute lymphoblastic leukemia.Cell death & disease · 2018Article
- DSSylation, a novel guide for protein degradation?Protein & cell · 2014Article
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14 authors at 5 institutions in 2 countries.
Funding
Abstract
Timely removal of oxidatively damaged proteins is critical for cells exposed to oxidative stresses; however, cellular mechanism for clearing oxidized proteins is not clear. Our study reveals a novel type of protein modification that may play a role in targeting oxidized proteins and remove them. In this process, DSS1 (deleted in split hand/split foot 1), an evolutionally conserved small protein, is conjugated to proteins induced by oxidative stresses in vitro and in vivo, implying oxidized proteins are DSS1 clients. A subsequent ubiquitination targeting DSS1-protein adducts has been observed, suggesting the client proteins are degraded through the ubiquitin-proteasome pathway. The DSS1 attachment to its clients is evidenced to be an enzymatic process modulated by an unidentified ATPase. We name this novel protein modification as DSSylation, in which DSS1 plays as a modifier, whose attachment may render target proteins a signature leading to their subsequent ubiquitination, thereby recruits proteasome to degrade them.
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