ArticlePLoS pathogens2018
Proteasome-associated HECT-type ubiquitin ligase activity is required for plant immunity.
Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 65 citations in OpenAlex.
- Ubiquitination-Mediated Regulation of Brassinosteroid Signaling.Plants (Basel, Switzerland) · 2026Review
- Ubiquitin-Mediated Proteolysis as a Regulator of the Plant Defense-Growth Balance.Plants (Basel, Switzerland) · 2026Review
- Development and selection of stably expressed reference genes for expression normalization in Ribes odoratum under drought stress.Scientific reports · 2025Article
- UPL3 promotes BZR1 degradation, growth arrest, and seedling survival under starvation stress in Arabidopsis.Plant communications · 2025Article
- The deubiquitinase Rpn11 functions as an allosteric ubiquitin sensor to promote substrate engagement by the 26S proteasome.Cell reports · 2025Article
- Deciphering the mechanism of E3 ubiquitin ligases in plant responses to abiotic and biotic stresses and perspectives on PROTACs for crop resistance.Plant biotechnology journal · 2024Review
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- Article
- Arabidopsis HECT and RING-type E3 Ligases Promote MAPKKK18 Degradation to Regulate Abscisic Acid Signaling.Plant & cell physiology · 2024Article
- Expression Profiling Reveals the Possible Involvement of the Ubiquitin-Proteasome Pathway in Abiotic Stress Regulation inInternational journal of molecular sciences · 2023Article
- Calcyclin-binding protein-promoted degradation of MdFRUCTOKINASE2 regulates sugar homeostasis in apple.Plant physiology · 2023Article
- Analysis of Proteasome-Associated Ubiquitin Ligase Activity.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators.Science advances · 2022Article
- The Ubiquitin-Proteasome System (UPS) and Viral Infection in Plants.Plants (Basel, Switzerland) · 2022Review
- HECT ubiquitin ligases as accessory proteins of the plant proteasome.Essays in biochemistry · 2022Article
- Harnessing the ubiquitin code to respond to environmental cues.Essays in biochemistry · 2022Article
- Ubiquitome profiling reveals a regulatory pattern of UPL3 with UBP12 on metabolic-leaf senescence.Life science alliance · 2022Article
- Pathogen exposure leads to a transcriptional downregulation of core cellular functions that may dampen the immune response in a macroalga.Molecular ecology · 2022Article
- Establishment of a Landscape of UPL5-Ubiquitinated on Multiple Subcellular Components of Leaf Senescence Cell inInternational journal of molecular sciences · 2022Article
- Serratia marcescens-S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70-2 in Nicotiana benthamiana.Microbial biotechnology · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Regulated degradation of proteins by the 26S proteasome plays important roles in maintenance and signalling in eukaryotic cells. Proteins are marked for degradation by the action of E3 ligases that site-specifically modify their substrates by adding chains of ubiquitin. Innate immune signalling in plants is deeply reliant on the ubiquitin-26S proteasome system. While progress has been made in understanding substrate ubiquitination during plant immunity, how these substrates are processed upon arrival at the proteasome remains unclear. Here we show that specific members of the HECT domain-containing family of ubiquitin protein ligases (UPL) play important roles in proteasomal substrate processing during plant immunity. Mutations in UPL1, UPL3 and UPL5 significantly diminished immune responses activated by the immune hormone salicylic acid (SA). In depth analyses of upl3 mutants indicated that these plants were impaired in reprogramming of nearly the entire SA-induced transcriptome and failed to establish immunity against a hemi-biotrophic pathogen. UPL3 was found to physically interact with the regulatory particle of the proteasome and with other ubiquitin-26S proteasome pathway components. In agreement, we demonstrate that UPL3 enabled proteasomes to form polyubiquitin chains, thereby regulating total cellular polyubiquitination levels. Taken together, our findings suggest that proteasome-associated ubiquitin ligase activity of UPL3 promotes proteasomal processivity and is indispensable for development of plant immunity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.