Overexpression of tomato RING E3 ubiquitin ligase gene SlRING1 confers cadmium tolerance by attenuating cadmium accumulation and oxidative stress

2020 ◽  
Author(s):  
Golam Jalal Ahammed ◽  
Cai‐Xia Li ◽  
Xin Li ◽  
Airong Liu ◽  
Shuangchen Chen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Cadmium Accumulation ◽  
Cadmium Tolerance ◽  
Ring E3 ◽  
And Oxidative Stress

scholarly journals The von Hippel–Lindau Cullin-RING E3 ubiquitin ligase regulates APOBEC3 cytidine deaminases

2021 ◽  
Author(s):  
Gaël K. Scholtès ◽  
Aubrey M. Sawyer ◽  
Cristina C. Vaca ◽  
Isabelle Clerc ◽  
Meejeon Roh ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Cytidine Deaminases ◽  
Von Hippel Lindau ◽  
Ring E3

scholarly journals Identification of a PGXPP degron motif in dishevelled and structural basis for its binding to the E3 ligase KLHL12

Open Biology ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 200041 ◽  
Author(s):  
Zhuoyao Chen ◽  
Gregory A. Wasney ◽  
Sarah Picaud ◽  
Panagis Filippakopoulos ◽  
Masoud Vedadi ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Molecular Mechanisms ◽  
Hydrophobic Interactions ◽  
E3 Ubiquitin Ligase ◽  
Structural Basis ◽  
E3 Ligases ◽  
Kelch Domain ◽  
Ring E3 Ligases ◽  
Ring E3 ◽  
New Protein

Wnt signalling is dependent on dishevelled proteins (DVL1-3), which assemble an intracellular Wnt signalosome at the plasma membrane. The levels of DVL1-3 are regulated by multiple Cullin-RING E3 ligases that mediate their ubiquitination and degradation. The BTB-Kelch protein KLHL12 was the first E3 ubiquitin ligase to be identified for DVL1-3, but the molecular mechanisms determining its substrate interactions have remained unknown. Here, we mapped the interaction of DVL1-3 to a ‘PGXPP' motif that is conserved in other known partners and substrates of KLHL12, including PLEKHA4, PEF1, SEC31 and DRD4. To determine the binding mechanism, we solved a 2.4 Å crystal structure of the Kelch domain of KLHL12 in complex with a DVL1 peptide that bound with low micromolar affinity. The DVL1 substrate adopted a U-shaped turn conformation that enabled hydrophobic interactions with all six blades of the Kelch domain β-propeller. In cells, the mutation or deletion of this motif reduced the binding and ubiquitination of DVL1 and increased its stability confirming this sequence as a degron motif for KLHL12 recruitment. These results define the molecular mechanisms determining DVL regulation by KLHL12 and establish the KLHL12 Kelch domain as a new protein interaction module for a novel proline-rich motif.

scholarly journals TFEB activates Nrf2 by repressing its E3 ubiquitin ligase DCAF11 and promoting phosphorylation of p62

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Jee-Yun Park ◽  
Sunhyo Kim ◽  
Hee Young Sohn ◽  
Young Ho Koh ◽  
Chulman Jo
Keyword(s):  
Oxidative Stress ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Biological Response ◽  
Related Factor ◽  
Mrna Levels ◽  
Nuclear Factor ◽  
Glutathione S Transferase ◽  
First Time ◽  
Cellular Stressors

Abstract Transcriptional factor EB (TFEB) and nuclear factor E2-related factor 2 (Nrf2) play crucial roles in the biological response against cellular stressors; however, their relationship has not yet been investigated. Here, we constructed human neuroglioma cell lines stably expressing TFEB. The expression of Nrf2-response genes, including heme oxygenase (HO)-1, glutathione-s-transferase-mu1 (GSTM1), and p62, was induced in the cell line, independent of oxidative stress. Of note, the protein level of Nrf2 was significantly increased, and its ubiquitinated fraction was reduced in stable cells compared to that in the control cells. Among E3 ubiquitin ligases known to be involved in the ubiquitination of Nrf2, DDB1 and Cullin4 associated factor 11 (DCAF11) was down-regulated at both protein and mRNA levels in stable cells, indicating that the repression of DCAF11 by TFEB may be mainly involved in the stabilization of Nrf2. In addition, the level of phosphorylated p62 at S349 was highly increased in stable cells compared to that in control cells, which could allow it to interfere with the association of Keap1 and Nrf2, thus stabilizing Nrf2. We suggest for the first time that TFEB could activate Nrf2 by increasing its stability under conditions devoid of oxidative stress.

scholarly journals Modulation of Phototropic Responsiveness in Arabidopsis through Ubiquitination of Phototropin 1 by the CUL3-Ring E3 Ubiquitin Ligase CRL3NPH3

2011 ◽  
Vol 23 (10) ◽  
pp. 3627-3640 ◽  
Author(s):  
Diana Roberts ◽  
Ullas V. Pedmale ◽  
Johanna Morrow ◽  
Shrikesh Sachdev ◽  
Esther Lechner ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring E3

scholarly journals The Cullin-RING E3 Ubiquitin Ligase CRL4−DCAF1 Complex Dimerizes via a Short Helical Region in DCAF1

Biochemistry ◽  
2011 ◽  
Vol 50 (8) ◽  
pp. 1359-1367 ◽  
Author(s):  
Jinwoo Ahn ◽  
Zach Novince ◽  
Jason Concel ◽  
Chang-Hyeock Byeon ◽  
Alexander M. Makhov ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring E3 ◽  
Helical Region
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