ArticlePLoS pathogens2020
Ubiquitin-Like protein 5 interacts with the silencing suppressor p3 of rice stripe virus and mediates its degradation through the 26S proteasome pathway.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- 'Candidatus Liberibacter asiaticus' secretory protein SDE5640 activates host autophagy dependent on PSMD10 to mediate PBA1 degradation.The Plant journal : for cell and molecular biology · 2026Article
- The dehydrin protein COR15 enhances antiviral RNA silencing by preventing viral protein-mediated SGS3 degradation and promoting SGS3 condensate formation.Plant communications · 2026Article
- E3 ubiquitin ligases in plant defense: mechanisms and prospects for resistance breeding.Science China. Life sciences · 2026Review
- The Ubiquitin-Proteasome System Plays Dual Roles in Plant Antiviral Defense and Viral Pathogenicity.Plants (Basel, Switzerland) · 2026Review
- 'Candidatus Liberibacter asiaticus' Effector SDE4250 Targets Citrus Proteasome Protein RPN10 to Inhibit Salicylic Acid-Mediated Citrus Immunity.Molecular plant pathology · 2026Article
- Antiviral activity and mechanism of purine morpholine nucleoside analogues incorporating a sulfonamide fragment.Journal of advanced research · 2026Article
- Purα is an essential host factor for rice stripe virus accumulation and transmission in the small brown planthopper.Archives of virology · 2026Article
- RING-Between-RING-Type E3 Ligase Ariadne-Like Protein 8 Negatively Regulates Plant Virus Infection by Targeting a Viral Movement Protein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- RD21 enhances resistance to the strawberry vein banding virus by promoting autophagy-mediated degradation of the viral silencing suppressor P6 protein.Plant biotechnology journal · 2025Article
- Divide and survive: PuZFP1 coordinates dual root developmental pathways for drought adaptation in Populus.Plant physiology · 2025Article
- UBL5 and Its Role in Viral Infections.Viruses · 2024Review
- Crop antiviral defense: Past and future perspective.Science China. Life sciences · 2024Review
- Article
- Turnip mosaic virus NIb weakens the function of eukaryotic translation initiation factor 6 facilitating viral infection in Nicotiana benthamiana.Molecular plant pathology · 2024Article
- Rice stripe virus nonstructural protein 3 suppresses plant defence responses mediated by the MEL-SHMT1 module.Molecular plant pathology · 2023Article
- Evaluation of cucumber UBL5 promoter as a tool for transgene expression and genome editing in plants.Transgenic research · 2023Article
- The Great Game between Plants and Viruses: A Focus on Protein Homeostasis.International journal of molecular sciences · 2023Review
- Rice stripe virus p2 protein interacts with ATG5 and is targeted for degradation by autophagy.Frontiers in microbiology · 2023Article
- Comprehensive Analysis of Ubiquitome Changes inViruses · 2022Article
- Combined Proteomic and Metabolomic Analysis of the Molecular Mechanism Underlying the Response to Salt Stress during Seed Germination in Barley.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitin like protein 5 (UBL5) interacts with other proteins to regulate their function but differs from ubiquitin and other UBLs because it does not form covalent conjugates. Ubiquitin and most UBLs mediate the degradation of target proteins through the 26S proteasome but it is not known if UBL5 can also do that. Here we found that the UBL5s of rice and Nicotiana benthamiana interacted with rice stripe virus (RSV) p3 protein. Silencing of NbUBL5s in N. benthamiana facilitated RSV infection, while UBL5 overexpression conferred resistance to RSV in both N. benthamiana and rice. Further analysis showed that NbUBL5.1 impaired the function of p3 as a suppressor of silencing by degrading it through the 26S proteasome. NbUBL5.1 and OsUBL5 interacted with RPN10 and RPN13, the receptors of ubiquitin in the 26S proteasome. Furthermore, silencing of NbRPN10 or NbRPN13 compromised the degradation of p3 mediated by NbUBL5.1. Together, the results suggest that UBL5 mediates the degradation of RSV p3 protein through the 26S proteasome, a previously unreported plant defense strategy against RSV infection.
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