scholarly journals The Arabidopsis C3H2C3-Type RING E3 Ubiquitin Ligase AtAIRP1 Is a Positive Regulator of an Abscisic Acid-Dependent Response to Drought Stress

2010 ◽  
Vol 154 (4) ◽  
pp. 1983-1997 ◽  
Author(s):  
Moon Young Ryu ◽  
Seok Keun Cho ◽  
Woo Taek Kim
Keyword(s):  
Abscisic Acid ◽  
Drought Stress ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Positive Regulator ◽  
Ring E3

scholarly journals The Arabidopsis RING E3 Ubiquitin Ligase AtAIRP2 Plays Combinatory Roles with AtAIRP1 in Abscisic Acid-Mediated Drought Stress Responses

2011 ◽  
Vol 157 (4) ◽  
pp. 2240-2257 ◽  
Author(s):  
Seok Keun Cho ◽  
Moon Young Ryu ◽  
Dong Hye Seo ◽  
Bin Goo Kang ◽  
Woo Taek Kim
Keyword(s):  
Abscisic Acid ◽  
Drought Stress ◽  
Ubiquitin Ligase ◽  
Stress Responses ◽  
E3 Ubiquitin Ligase ◽  
Ring E3

AtKPNB1, an Arabidopsis importin-β protein, is downstream of the RING E3 ubiquitin ligase AtAIRP1 in the ABA-mediated drought stress response

Planta ◽  
2020 ◽  
Vol 252 (5) ◽  
Author(s):  
Tae Rin Oh ◽  
Seong Gwan Yu ◽  
Hee Woong Yang ◽  
Jong Hum Kim ◽  
Woo Taek Kim
Keyword(s):  
Drought Stress ◽  
Stress Response ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Β Protein ◽  
Ring E3

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.

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