The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Wheat RING E3 ubiquitin ligase TaDIS1 degrade TaSTP via the 26S proteasome pathway
Abstract
Drought stress has a great impact on wheat yields. The ubiquitin/26S proteasome system is one of the most important mechanisms employed by plants for responding to stress. E3 ubiquitin ligase is an important part of the ubiquitin/26S proteasome system. In wheat, the mechanism of E3 ubiquitin ligase TaDIS1 has not been investigated in great detail. In this study, TaSTP was identified as an interacting partner using yeast two-hybrid screening. The results obtained from bimolecular fluorescence complementation, pull-down, and co-immunoprecipitation assays also demonstrated that TaDIS1 interacts with TaSTP. In vitro ubiquitination assays showed that TaDIS1 has an E3 ubiquitin ligase activity and the results based on two TaDIS1 mutants suggested that the RING domain is essential for its E3 ubiquitin ligase activity. In addition, we used MG132 to show that TaSTP can be degraded by TaDIS1 via the 26S proteasome pathway. The transcript levels of TaSTP showed that it can also respond to different abiotic stresses, such as drought, salt, and abscisic acid treatment. RING E3 ubiquitin ligase TaDIS1 may through the posttranslational regulation of TaSTP to play an important role in drought tolerance.
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“Based on previous reports, multiple homologs of these genes were found to be involved in plant biotic stress and stress-resistance processes [26,27,28,29,30,31].”
From Transcriptome-Based WGCNA Analysis Reveals the Mechanism of Drought Resistance Differences in Sweetpotato (Ipomoea batatas (L.) Lam.) (2023) · cites this paper as [30]
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Cites
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860
A QTL for rice grain width and weight encodes a previously unknown RING-type E3 ubiquitin ligase
Song, X., Huang, W., Shi, M., Zhu, M., & Lin, H. (2007) · Nature Genetics · doi:10.1038/ng2014 · Cited by 1,660
The ubiquitin–proteasome pathway: on protein death and cell life
Ciechanover, A. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7151 · Cited by 1,419
THE UBIQUITIN 26S PROTEASOME PROTEOLYTIC PATHWAY
Smalle, J., & Vierstra, R. D. (2004) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.55.031903.141801 · Cited by 1,357
The ubiquitin–26S proteasome system at the nexus of plant biology
Vierstra, R. D. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2688 · Cited by 1,343
Functional Analysis of the RING-Type Ubiquitin Ligase Family of Arabidopsi s
Stone, S. L., Hauksdóttir, H., Troy, A., Herschleb, J., Kraft, E., & Callis, J. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.052423 · Cited by 628
Uemura, T., Ueda, T., Ohniwa, R. L., Nakano, A., Takeyasu, K., & Sato, M. H. (2004) · Cell Structure and Function · doi:10.1247/csf.29.49 · Cited by 532
Qin, F., Sakuma, Y., Tran, L. P., Maruyama, K., Kidokoro, S., Fujita, Y., Fujita, M., Umezawa, T., Sawano, Y., Miyazono, K., et al. (2008) · The Plant Cell · doi:10.1105/tpc.107.057380 · Cited by 528
The Cullin-RING Ubiquitin-Protein Ligases
Hua, Z., & Vierstra, R. D. (2011) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112256 · Cited by 524
The AIP2 E3 ligase acts as a novel negative regulator of ABA signaling by promoting ABI3 degradationPreprint
Zhang, X., Garretón, V., & Chua, N. (2005) · Genes & Development · doi:10.1101/gad.1318705 · Cited by 438
Research works printed but not linked: 2
- Yu, 2013, The Chinese wild grapevine (Vitis pseudoreticulata) E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) activates plant defense responses by inducing proteolysis of the VpWRKY11 transcription factor, New Phytol., 200, 834, 10.1111/nph.12418 · DOI
- Ning, 2011, The SINA E3 ligase OsDIS1 negatively regulates drought response in rice, Plant Physiol., 157, 242, 10.1104/pp.111.180893 · DOI
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RING Zinc Finger Proteins in Plant Abiotic Stress Tolerance
Han, G., Qiao, Z., Li, Y., Yang, Z., Wang, C., Zhang, Y., Liu, L., & Wang, B. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.877011 · Cited by 101
Review: Biological functions of major latex-like proteins in plants
Fujita, K., & Inui, H. (2021) · Plant Science · doi:10.1016/j.plantsci.2021.110856 · Cited by 69
Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses
Wang, S., Lv, X., Zhang, J., Chen, D., Chen, S., Fan, G., Ma, C., & Wang, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042308 · Cited by 65
Role of ubiquitination enzymes in abiotic environmental interactions with plants
Sharma, S., Prasad, A., Sharma, N., & Prasad, M. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.03.185 · Cited by 49
Xu, J., Liu, H., Zhou, C., Wang, J., Wang, J., Han, Y., Zheng, N., Zhang, M., & Li, X. (2024) · Plant Science · doi:10.1016/j.plantsci.2024.112035 · Cited by 51
Self-citation
Metadata
- Authors
- Lv, Q., Zhang, L., Zan, T., Li, L., & Li, X.
- Affiliations
- Northwest A&F University (CN)
- Corresponding author
- Li, Xuejun
- ORCID
- Li, Liqun
- Venue
- Plant Science
- Publisher
- Elsevier BV
- Published
- 2020-07
- Volume
- 296
- Pages
- 110494
- ISSN
- 0168-9452 (ISSN-L)
- OpenAlex
- W3018683072
- Cited by
- 29
- References
- 46
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 8 · 2023: 5 · 2022: 5 · 2021: 5
- FWCI
- 1.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Plant Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Key R&D Program of China (2017YFD0100704)
- National Special Program for Transgenetic Wheat Breeding (2016ZX08002003)
- State Administration of Foreign Experts Affairs (#B18042)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- RING E3 ubiquitin ligase, 26S proteasome, protein degradation, drought tolerance, wheat, protein-protein interaction, abiotic stress response, abscisic acid, salt stress, post-translational regulation
- MeSH terms
- Cloning, Molecular, Dehydration, Plant Proteins, Triticum, Gene Expression Regulation, Plant, Two-Hybrid System Techniques, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Immunoprecipitation, Metabolic Networks and Pathways
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- Lv, Q., Zhang, L., Zan, T., Li, L., & Li, X. (2020). Wheat RING E3 ubiquitin ligase TaDIS1 degrade TaSTP via the 26S proteasome pathway. Plant Science. https://doi.org/10.1016/j.plantsci.2020.110494
