ArticleJournal of visualized experiments : JoVE2014
Assaying proteasomal degradation in a cell-free system in plants.
Article in Journal of visualized experiments : JoVE, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- ANAPHASE-PROMOTING COMPLEX/CYCLOSOME coactivators maintain AURORA 1 kinase homeostasis during meiotic chromosome segregation.The Plant cell · 2025Article
- HEI10 is subject to phase separation and mediates RPA1a degradation during meiotic interference-sensitive crossover formation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- GhXB38D represses cotton fibre elongation through ubiquitination of ethylene biosynthesis enzymes GhACS4 and GhACO1.Plant biotechnology journal · 2023Article
- Article
- E3 ligase, the Oryza sativa salt-induced RING finger protein 4 (OsSIRP4), negatively regulates salt stress responses via degradation of the OsPEX11-1 protein.Plant molecular biology · 2021Article
- Molecular characterization of a RING E3 ligase SbHCI1 in sorghum under heat and abscisic acid stress.Planta · 2020Article
- MaXB3 Modulates MaNAC2, MaACS1, and MaACO1 Stability to Repress Ethylene Biosynthesis during Banana Fruit Ripening.Plant physiology · 2020Article
- Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression.Plant molecular biology · 2020Article
- Oryza sativa heat-induced RING finger protein 1 (OsHIRP1) positively regulates plant response to heat stress.Plant molecular biology · 2019Article
- The Agrobacterium F-Box Protein Effector VirF Destabilizes the Arabidopsis GLABROUS1 Enhancer/Binding Protein-Like Transcription Factor VFP4, a Transcriptional Activator of Defense Response Genes.Molecular plant-microbe interactions : MPMI · 2018Article
- Real-time monitoring of PtaHMGB activity in poplar transactivation assays.Plant methods · 2017Article
- The Banana Fruit SINA Ubiquitin Ligase MaSINA1 Regulates the Stability of MaICE1 to be Negatively Involved in Cold Stress Response.Frontiers in plant science · 2017Article
- A disulphide isomerase gene (PDI-V) from Haynaldia villosa contributes to powdery mildew resistance in common wheat.Scientific reports · 2016Article
- Association analysis for disease resistance to Fusarium oxysporum in cape gooseberry (Physalis peruviana L).BMC genomics · 2016Article
- Nopaline-type Ti plasmid of Agrobacterium encodes a VirF-like functional F-box protein.Scientific reports · 2015Article
- Interaction of Arabidopsis Trihelix-Domain Transcription Factors VFP3 and VFP5 with Agrobacterium Virulence Protein VirF.PloS one · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The ubiquitin-proteasome pathway for protein degradation has emerged as one of the most important mechanisms for regulation of a wide spectrum of cellular functions in virtually all eukaryotic organisms. Specifically, in plants, the ubiquitin/26S proteasome system (UPS) regulates protein degradation and contributes significantly to development of a wide range of processes, including immune response, development and programmed cell death. Moreover, increasing evidence suggests that numerous plant pathogens, such as Agrobacterium, exploit the host UPS for efficient infection, emphasizing the importance of UPS in plant-pathogen interactions. The substrate specificity of UPS is achieved by the E3 ubiquitin ligase that acts in concert with the E1 and E2 ligases to recognize and mark specific protein molecules destined for degradation by attaching to them chains of ubiquitin molecules. One class of the E3 ligases is the SCF (Skp1/Cullin/F-box protein) complex, which specifically recognizes the UPS substrates and targets them for ubiquitination via its F-box protein component. To investigate a potential role of UPS in a biological process of interest, it is important to devise a simple and reliable assay for UPS-mediated protein degradation. Here, we describe one such assay using a plant cell-free system. This assay can be adapted for studies of the roles of regulated protein degradation in diverse cellular processes, with a special focus on the F-box protein-substrate interactions.
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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.