Suppression of Arabidopsis RING-DUF1117 E3 ubiquitin ligases, AtRDUF1 and AtRDUF2, reduces tolerance to ABA-mediated drought stress

2012 ◽  
Vol 420 (1) ◽  
pp. 141-147 ◽  
Author(s):  
Soo Jin Kim ◽  
Moon Young Ryu ◽  
Woo Taek Kim
Keyword(s):  
Drought Stress ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases

scholarly journals Arabidopsis PUB22 and PUB23 Are Homologous U-Box E3 Ubiquitin Ligases That Play Combinatory Roles in Response to Drought Stress

2008 ◽  
Vol 20 (7) ◽  
pp. 1899-1914 ◽  
Author(s):  
Seok Keun Cho ◽  
Moon Young Ryu ◽  
Charlotte Song ◽  
June M. Kwak ◽  
Woo Taek Kim
Keyword(s):  
Drought Stress ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases

scholarly journals Molecular Characterization of U-Box E3 Ubiquitin Ligases (TaPUB2 and TaPUB3) Involved in the Positive Regulation of Drought Stress Response in Arabidopsis

2021 ◽  
Vol 22 (24) ◽  
pp. 13658
Author(s):  
Jae Ho Kim ◽  
Moon Seok Kim ◽  
Dae Yeon Kim ◽  
Joseph Noble Amoah ◽  
Yong Weon Seo
Keyword(s):  
Abiotic Stress ◽  
Drought Stress ◽  
Golgi Apparatus ◽  
Ubiquitin Ligase ◽  
Ubiquitin Ligases ◽  
Bimolecular Fluorescence Complementation ◽  
E3 Ubiquitin Ligases ◽  
Cellular Functions ◽  
Transient Expression Assay

Plant U-box E3 ubiquitin ligase (PUB) is involved in various environmental stress conditions. However, the molecular mechanism of U-box proteins in response to abiotic stress in wheat remains unknown. In this study, two U-box E3 ligase genes (TaPUB2 and TaPUB3), which are highly expressed in response to adverse abiotic stresses, were isolated from common wheat, and their cellular functions were characterized under drought stress. Transient expression assay revealed that TaPUB2 was localized in the cytoplasm and Golgi apparatus, whereas TaPUB3 was expressed only in the Golgi apparatus in wheat protoplasts. Additionally, TaPUB2 and TaPUB3 underwent self-ubiquitination. Moreover, TaPUB2/TaPUB3 heterodimer was identified in yeast and the cytoplasm of wheat protoplasts using a pull-down assay and bimolecular fluorescence complementation analysis. Heterogeneous overexpression of TaPUB2 and TaPUB3 conferred tolerance to drought stress. Taken together, these results implied that the heterodimeric form of U-box E3 ubiquitin ligases (TaPUB2/TaPUB3) responded to abiotic stress and roles as a positive regulator of drought stress tolerance.

scholarly journals The Arabidopsis paralogs, PUB46 and PUB48, encoding U-box E3 ubiquitin ligases, are essential for plant response to drought stress

2017 ◽  
Vol 17 (1) ◽  
Author(s):  
Guy Adler ◽  
Zvia Konrad ◽  
Lyad Zamir ◽  
Amit Kumar Mishra ◽  
Dina Raveh ◽  
...  
Keyword(s):  
Drought Stress ◽  
Ubiquitin Ligases ◽  
Plant Response ◽  
E3 Ubiquitin Ligases

scholarly journals Roles of Four Arabidopsis U-Box E3 Ubiquitin Ligases in Negative Regulation of Abscisic Acid-Mediated Drought Stress Responses

2012 ◽  
Vol 160 (1) ◽  
pp. 556-568 ◽  
Author(s):  
Dong Hye Seo ◽  
Moon Young Ryu ◽  
Fabien Jammes ◽  
Jae Hwan Hwang ◽  
Michelle Turek ◽  
...  
Keyword(s):  
Abscisic Acid ◽  
Drought Stress ◽  
Stress Responses ◽  
Ubiquitin Ligases ◽  
Negative Regulation ◽  
E3 Ubiquitin Ligases

scholarly journals Genome-Wide Identification of Soybean U-Box E3 Ubiquitin Ligases and Roles of GmPUB8 in Negative Regulation of Drought Stress Response in Arabidopsis

2016 ◽  
Vol 57 (6) ◽  
pp. 1189-1209 ◽  
Author(s):  
Ning Wang ◽  
Yaping Liu ◽  
Yahui Cong ◽  
Tingting Wang ◽  
Xiujuan Zhong ◽  
...  
Keyword(s):  
Drought Stress ◽  
Stress Response ◽  
Ubiquitin Ligases ◽  
Negative Regulation ◽  
E3 Ubiquitin Ligases ◽  
Genome Wide

Regulation of Epithelial-Mesenchymal Transition by E3 Ubiquitin Ligases and Deubiquitinase in Cancer

2016 ◽  
Vol 16 (2) ◽  
pp. 110-118 ◽  
Author(s):  
Yasumichi Inoue ◽  
Yuka Itoh ◽  
Koichi Sato ◽  
Fumihiro Kawasaki ◽  
Chihiro Sumita ◽  
...  
Keyword(s):  
Epithelial Mesenchymal Transition ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Mesenchymal Transition

scholarly journals Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1015
Author(s):  
Utsa Bhaduri ◽  
Giuseppe Merla
Keyword(s):  
Drug Discovery ◽  
Protein Degradation ◽  
Ubiquitin Ligase ◽  
Genetic Disorders ◽  
E3 Ubiquitin Ligase ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Post Translational Modification ◽  
Disease Biology ◽  
The Future

Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite motif (TRIM) family proteins are known to have proven E3 ubiquitin ligase activities and are involved in a multitude of cellular and physiological events and pathophysiological conditions ranging from cancers to rare genetic disorders. Although in recent years many kinds of E3 ubiquitin ligases have emerged as the preferred choices of big pharma and biotech startups in the context of protein degradation and disease biology, from a surface overview it appears that TRIM E3 ubiquitin ligases are not very well recognized yet in the realm of drug discovery. This article will review some of the blockbuster scientific discoveries and technological innovations from the world of ubiquitination and E3 ubiquitin ligases that have impacted the biopharma community, from biotech colossuses to startups, and will attempt to evaluate the future of TRIM family proteins in the province of E3 ubiquitin ligase-based drug discovery.

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