scholarly journals FLYING SAUCER1 Is a Transmembrane RING E3 Ubiquitin Ligase That Regulates the Degree of Pectin Methylesterification in Arabidopsis Seed Mucilage

2013 ◽  
Vol 25 (3) ◽  
pp. 944-959 ◽  
Author(s):  
Cătălin Voiniciuc ◽  
Gillian H. Dean ◽  
Jonathan S. Griffiths ◽  
Kerstin Kirchsteiger ◽  
Yeen Ting Hwang ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Arabidopsis Seed ◽  
Ring E3 ◽  
Seed Mucilage

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 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

scholarly journals Cross-species analysis of LZTR1 loss-of-function mutants demonstrates dependency to RIT1 orthologs

2022 ◽  
Author(s):  
Antonio Cuevas-Navarro ◽  
Laura Rodriguez-Muñoz ◽  
Joaquim Grego-Bessa ◽  
Alice Cheng ◽  
Katherine A Rauen ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Null Allele ◽  
E3 Ubiquitin Ligase ◽  
Adaptor Protein ◽  
Loss Of Function ◽  
Ras Gtpases ◽  
Ubiquitin Ligase Complex ◽  
Species Analysis ◽  
Cullin 3 ◽  
Ring E3

RAS GTPases are highly conserved proteins involved in the regulation of mitogenic signaling. We have previously described a novel Cullin 3 RING E3 ubiquitin ligase complex formed by the substrate adaptor protein LZTR1 that binds, ubiquitinates, and promotes proteasomal degradation of the RAS GTPase RIT1. In addition, others have described that this complex is also responsible for the ubiquitination of canonical RAS GTPases. Here, we have analyzed the phenotypes of LZTR1 loss-of-function mutants in both fruit flies and mice and have demonstrated biochemical dependency on their RIT1 orthologs. Moreover, we show that LZTR1 is haplosufficient in mice and that embryonic lethality of the homozygous null allele can be rescued by deletion of RIT1.

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