scholarly journals Correction: A Ubiquitin Ligase Complex Regulates Caspase Activation During Sperm Differentiation in Drosophila

PLoS Biology ◽  
2007 ◽  
Vol 5 (11) ◽  
pp. e291
Author(s):  
Eli Arama ◽  
Maya Bader ◽  
Gabrielle E Rieckhof ◽  
Hermann Stellar
Keyword(s):  
Ubiquitin Ligase ◽  
Caspase Activation ◽  
Ubiquitin Ligase Complex

scholarly journals A Ubiquitin Ligase Complex Regulates Caspase Activation During Sperm Differentiation in Drosophila

PLoS Biology ◽  
2007 ◽  
Vol 5 (10) ◽  
pp. e251 ◽  
Author(s):  
Eli Arama ◽  
Maya Bader ◽  
Gabrielle E Rieckhof ◽  
Hermann Steller
Keyword(s):  
Ubiquitin Ligase ◽  
Caspase Activation ◽  
Ubiquitin Ligase Complex

COI1 links jasmonate signalling and fertility to the SCF ubiquitin-ligase complex inArabidopsis

2002 ◽  
Vol 32 (4) ◽  
pp. 457-466 ◽  
Author(s):  
Alessandra Devoto ◽  
Manuela Nieto-Rostro ◽  
Daoxin Xie ◽  
Christine Ellis ◽  
Rebecca Harmston ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Ubiquitin Ligase Complex ◽  
Scf Ubiquitin Ligase ◽  
Jasmonate Signalling

scholarly journals Lunapark Is a Component of a Ubiquitin Ligase Complex Localized to the Endoplasmic Reticulum Three-way Junctions

2016 ◽  
Vol 291 (35) ◽  
pp. 18252-18262 ◽  
Author(s):  
Yupeng Zhao ◽  
Ting Zhang ◽  
Huanhuan Huo ◽  
Yihong Ye ◽  
Yanfen Liu
Keyword(s):  
Endoplasmic Reticulum ◽  
Ubiquitin Ligase ◽  
Ubiquitin Ligase Complex

scholarly journals An intracellular pathogen response pathway promotes proteostasis in C. elegans

2017 ◽  
Author(s):  
Kirthi C. Reddy ◽  
Tal Dror ◽  
Jessica N. Sowa ◽  
Johan Panek ◽  
Kevin Chen ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Intracellular Pathogen ◽  
Forward Genetic Screen ◽  
C Elegans ◽  
Transcriptional Signature ◽  
Proteotoxic Stress ◽  
Ubiquitin Ligase Complex ◽  
Pathogen Response ◽  
Mutant Phenotypes ◽  
Increased Activity

SummaryMaintenance of proteostasis is critical for organismal health. Here we describe a novel pathway that promotes proteostasis, identified through the analysis of C. elegans genes upregulated by intracellular infection. We named this distinct transcriptional signature the Intracellular Pathogen Response (IPR), and it includes upregulation of several predicted ubiquitin ligase complex components such as the cullin cul-6. Through a forward genetic screen we found pals-22, a gene of previously unknown function, to be a repressor of the cul-6/Cullin gene and other IPR gene expression. Interestingly, pals-22 mutants have increased thermotolerance and reduced levels of stress-induced polyglutamine aggregates, likely due to upregulated IPR expression. We found the enhanced stress resistance of pals-22 mutants to be dependent on cul-6, suggesting that pals-22 mutants have increased activity of a CUL-6/Cullin-containing ubiquitin ligase complex. pals-22 mutant phenotypes are distinct from the well-studied heat shock and insulin signaling pathways, indicating that the IPR is a novel pathway that protects animals from proteotoxic stress.

scholarly journals PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex

2008 ◽  
Vol 22 (18) ◽  
pp. 2496-2506 ◽  
Author(s):  
T. Abbas ◽  
U. Sivaprasad ◽  
K. Terai ◽  
V. Amador ◽  
M. Pagano ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Ubiquitin Ligase Complex
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