scholarly journals SPA Proteins Affect the Subcellular Localization of COP1 in the COP1/SPA Ubiquitin Ligase Complex during Photomorphogenesis

2017 ◽  
Vol 174 (3) ◽  
pp. 1314-1321 ◽  
Author(s):  
Martin Balcerowicz ◽  
Konstantin Kerner ◽  
Christian Schenkel ◽  
Ute Hoecker
Keyword(s):  
Subcellular Localization ◽  
Ubiquitin Ligase ◽  
Ubiquitin Ligase Complex ◽  
Spa Proteins

scholarly journals Direct phosphorylation of HY5 by SPA1 kinase to regulate photomorphogenesis in Arabidopsis

2020 ◽  
Author(s):  
Wenli Wang ◽  
Inyup Paik ◽  
Junghyun Kim ◽  
Xilin Hou ◽  
Sibum Sung ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Active Form ◽  
E3 Ubiquitin Ligase ◽  
Kinase Domain ◽  
Ubiquitin Ligase Complex ◽  
The Stability ◽  
Target Promoters ◽  
Spa Proteins

SUMMARYELONGATED HYPOCOTYL5 (HY5) is a key transcription factor which promotes photomorphogenesis by regulating complex downstream growth programs. Previous studies suggest that the regulation of HY5 mainly depends on the CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1) - SUPPRESSOR OF PHYTOCHROME A-105 (SPA) E3 ubiquitin ligase complex, which degrades positively acting transcription factors of light signaling to repress photomorphogenesis in the dark. SPA proteins function not only as a component of the E3 ubiquitin ligase complex but also as a kinase of PHYTOCHROME INTERACTING FACTOR1 (PIF1) through its N-terminal kinase domain. Here, we show that HY5 is a new substrate of SPA1 kinase. SPA1 can directly phosphorylate HY5 in vitro and in vivo. We also demonstrate that unphosphorylated HY5 strongly interacts with both COP1 and SPA1 than phosphorylated HY5, is the preferred substrate for degradation, whereas phosphorylated HY5 is more stable in the dark. In addition, unphosphorylated HY5 actively binds to the target promoters, and is physiologically more active form. Consistently, the transgenic plants expressing unphosphorylated mutant of HY5 displays enhanced photomorphogenesis. Collectively, our study revealed that SPA1 fine-tunes the stability and the activity of HY5 to regulate photomorphogenesis.

Protein interactions and subcellular localization in S-RNase-based self-incompatibility

2010 ◽  
Vol 38 (2) ◽  
pp. 622-626 ◽  
Author(s):  
Thomas L. Sims ◽  
Avani Patel ◽  
Pratima Shrestha
Keyword(s):  
Subcellular Localization ◽  
Ubiquitin Ligase ◽  
Protein Interactions ◽  
Self Incompatibility ◽  
Exact Role ◽  
Complex Needs ◽  
Vacuolar Compartment ◽  
Ubiquitin Ligase Complex ◽  
Compatible Pollen

The recent identification of several proteins playing key roles in S-RNase-based gametophytic self-incompatibility has led both to a greater understanding of the molecular biology of this response, as well as to questions regarding the precise mechanism by which compatible pollen tubes are recognized and accepted. A proposed variant SCFSLF (where SCF is SSK1/cullin/F-box and SLF is S-locus F-box) ubiquitin ligase complex is thought to play a central role in recognizing and inhibiting non-self S-RNases, but the exact role of ubiquitination remains unclear. How the possible sequestration of non-self S-RNases in a pollen vacuolar compartment can be reconciled with the need for protein interaction between S-RNase and the SCFSLF complex needs to be determined. Current work to answer these questions focuses on more precisely defining quantitative protein interactions and subcellular localization of proteins involved in S-RNase-based gametophytic self-incompatibility.

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 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 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.

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