ArticleThe Plant cell2011
The defective proteasome but not substrate recognition function is responsible for the null phenotypes of the Arabidopsis proteasome subunit RPN10.
Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.
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Who cites it
41 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.
- Meta-analysis fails to show any correlation between protein abundance and ubiquitination changes.FEBS open bio · 2026Pooled it
- A wheat-specific proline-rich protein regulates grain weight through a ubiquitin-mediated delay of endosperm cellularization.The Plant journal : for cell and molecular biology · 2026Article
- Arabidopsis WSS1A, a DNA-protein crosslink repair protease, delays leaf senescence in cooperation with SUMO3.The Plant journal : for cell and molecular biology · 2026Article
- Jasmonate signaling and prey nutrient availability trigger distinct biochemical responses in the Drosera capensis feeding cycle.Plant physiology · 2026Article
- DSK2-mediated degradation of F-box protein LAO1 and class I TCPs modulates the nitrogen starvation response.EMBO reports · 2025Article
- The Structural Role of RPN10 in the 26S Proteasome and an RPN2-Binding Residue on RPN13 Are Functionally Important in Arabidopsis.International journal of molecular sciences · 2024Article
- Potential Role of Lysine Acetylation and Autophagy in Brown Film Formation and Postripening of Lentinula edodes Mycelium.Microbiology spectrum · 2023Article
- The Arabidopsis Deubiquitylase OTU5 Suppresses Flowering by Histone Modification-Mediated Activation of the Major Flowering RepressorsInternational journal of molecular sciences · 2023Article
- Comparative Ubiquitination Proteomics Revealed the Salt Tolerance Mechanism in Sugar Beet Monomeric Additional Line M14.International journal of molecular sciences · 2022Article
- Ubiquitin receptors play redundant roles in the proteasomal degradation of the p53 repressor MDM2.FEBS letters · 2022Article
- The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence.Communications biology · 2022Article
- Review
- The F-box E3 ubiquitin ligase BAF1 mediates the degradation of the brassinosteroid-activated transcription factor BES1 through selective autophagy in Arabidopsis.The Plant cell · 2021Article
- Article
- Leaf senescence: progression, regulation, and application.Molecular horticulture · 2021Review
- Multiple Layers of Regulation on Leaf Senescence: New Advances and Perspectives.Frontiers in plant science · 2021Review
- Emerging Roles of the Selective Autophagy in Plant Immunity and Stress Tolerance.International journal of molecular sciences · 2020Review
- Brassinosteroids: Multidimensional Regulators of Plant Growth, Development, and Stress Responses.The Plant cell · 2020Review
- NaCl-responsive ROS scavenging and energy supply in alkaligrass callus revealed from proteomic analysis.BMC genomics · 2019Article
- Proteomic analysis of affinity-purified 26S proteasomes identifies a suite of assembly chaperones inThe Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitylated substrate recognition during ubiquitin/proteasome-mediated proteolysis (UPP) is mediated directly by the proteasome subunits RPN10 and RPN13 and indirectly by ubiquitin-like (UBL) and ubiquitin-associated (UBA) domain-containing factors. To dissect the complexity and functional roles of UPP substrate recognition in Arabidopsis thaliana, potential UPP substrate receptors were characterized. RPN10 and members of the UBL-UBA-containing RAD23 and DSK2 families displayed strong affinities for Lys-48-linked ubiquitin chains (the major UPP signals), indicating that they are involved in ubiquitylated substrate recognition. Additionally, RPN10 uses distinct interfaces as primary proteasomal docking sites for RAD23s and DSK2s. Analyses of T-DNA insertion knockout or RNA interference knockdown mutants of potential UPP ubiquitin receptors, including RPN10, RPN13, RAD23a-d, DSK2a-b, DDI1, and NUB1, demonstrated that only the RPN10 mutant gave clear phenotypes. The null rpn10-2 showed decreased double-capped proteasomes, increased 20S core complexes, and pleiotropic vegetative and reproductive growth phenotypes. Surprisingly, the observed rpn10-2 phenotypes were rescued by a RPN10 variant defective in substrate recognition, indicating that the defectiveness of RPN10 in proteasome but not substrate recognition function is responsible for the null phenotypes. Our results suggest that redundant recognition pathways likely are used in Arabidopsis to target ubiquitylated substrates for proteasomal degradation and that their specific roles in vivo require further examination.
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