The rice RING E3 ligase, OsCTR1, inhibits trafficking to the chloroplasts of OsCP12 and OsRP1, and its overexpression confers drought tolerance inArabidopsis

2013 ◽  
Vol 37 (5) ◽  
pp. 1097-1113 ◽  
Author(s):  
SUNG DON LIM ◽  
CHANHUI LEE ◽  
CHEOL SEONG JANG
Keyword(s):  
Drought Tolerance ◽  
E3 Ligase ◽  
Ring E3 Ligase ◽  
Ring E3

scholarly journals A glycine-specific N-degron pathway mediates the quality control of protein N-myristoylation

Science ◽  
2019 ◽  
Vol 365 (6448) ◽  
pp. eaaw4912 ◽  
Author(s):  
Richard T. Timms ◽  
Zhiqian Zhang ◽  
David Y. Rhee ◽  
J. Wade Harper ◽  
Itay Koren ◽  
...  
Keyword(s):  
Quality Control ◽  
Protein Stability ◽  
Protein Degradation ◽  
E3 Ligase ◽  
Cleavage Sites ◽  
Caspase Cleavage ◽  
E3 Ligases ◽  
Ring E3 Ligase ◽  
The Stability ◽  
Ring E3

The N-terminal residue influences protein stability through N-degron pathways. We used stability profiling of the human N-terminome to uncover multiple additional features of N-degron pathways. In addition to uncovering extended specificities of UBR E3 ligases, we characterized two related Cullin-RING E3 ligase complexes, Cul2ZYG11B and Cul2ZER1, that act redundantly to target N-terminal glycine. N-terminal glycine degrons are depleted at native N-termini but strongly enriched at caspase cleavage sites, suggesting roles for the substrate adaptors ZYG11B and ZER1 in protein degradation during apoptosis. Furthermore, ZYG11B and ZER1 were found to participate in the quality control of N-myristoylated proteins, in which N-terminal glycine degrons are conditionally exposed after a failure of N-myristoylation. Thus, an additional N-degron pathway specific for glycine regulates the stability of metazoan proteomes.

scholarly journals Structure and dynamics of the ASB9 CUL-RING E3 Ligase

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Ryan J. Lumpkin ◽  
Richard W. Baker ◽  
Andres E. Leschziner ◽  
Elizabeth A. Komives
Keyword(s):  
E3 Ligase ◽  
Structure And Dynamics ◽  
Ring E3 Ligase ◽  
Ring E3

TRIM4; a novel mitochondrial interacting RING E3 ligase, sensitizes the cells to hydrogen peroxide (H2O2) induced cell death

2015 ◽  
Vol 89 ◽  
pp. 1036-1048 ◽  
Author(s):  
Dhanendra Tomar ◽  
Paresh Prajapati ◽  
Julie Lavie ◽  
Kritarth Singh ◽  
Sripada Lakshmi ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Cell Death ◽  
E3 Ligase ◽  
Ring E3 Ligase ◽  
Ring E3

scholarly journals The RING E3 Ligase KEEP ON GOING Modulates JASMONATE ZIM-DOMAIN12 Stability

2015 ◽  
Vol 169 (2) ◽  
pp. 1405-1417 ◽  
Author(s):  
Laurens Pauwels ◽  
Andrés Ritter ◽  
Jonas Goossens ◽  
Astrid Nagels Durand ◽  
Hongxia Liu ◽  
...  
Keyword(s):  
E3 Ligase ◽  
Ring E3 Ligase ◽  
Ring E3

scholarly journals Inactivation of the Cullin (CUL)-RING E3 ligase by the NEDD8-activating enzyme inhibitor MLN4924 triggers protective autophagy in cancer cells

Autophagy ◽  
2012 ◽  
Vol 8 (11) ◽  
pp. 1677-1679 ◽  
Author(s):  
Zhongguang Luo ◽  
Yongfu Pan ◽  
Lak Shin Jeong ◽  
Jie Liu ◽  
Lijun Jia
Keyword(s):  
Cancer Cells ◽  
Enzyme Inhibitor ◽  
E3 Ligase ◽  
Ring E3 Ligase ◽  
Ring E3
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