E3 Ubiquitin Ligase Nedd4‐2 Exerts Neuroprotective Effects During Endoplasmic Reticulum Stress

2021 ◽  
Author(s):  
Daphne E Lodes ◽  
Jiuhe Zhu ◽  
Nien‐Pei Tsai
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Neuroprotective Effects

scholarly journals Bajijiasu Ameliorates β-Amyloid-Triggered Endoplasmic Reticulum Stress and Related Pathologies in an Alzheimer’s Disease Model

2018 ◽  
Vol 46 (1) ◽  
pp. 107-117 ◽  
Author(s):  
Ting-Ting Xu ◽  
Yang Zhang ◽  
Jia-Yang He ◽  
Dan Luo ◽  
Yi Luo ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Western Blotting ◽  
Disease Model ◽  
Beta Amyloid ◽  
Amyloid Peptide ◽  
Neuroprotective Effects ◽  
Beneficial Effects ◽  
Y Maze ◽  
Improved Learning

Background/Aims: Alzheimer disease (AD) is a common neurodegenerative disease that is characterized by the deposition of beta-amyloid peptide and formation of intracellular neurofibrillary tangles. Due to the failure of various clinical trials of novel drugs for AD, effective drugs for AD treatment are urgently required. Methods: In this study, we used the classic APP/PS1 mouse model to explore the neuroprotective effects of a new compound, bajijiasu, and the mechanisms involved. Behavioral tests and western blotting were performed to assess the beneficial effects of bajijiasu in APP/PS1 mice. Results: Morris water maze and Y-maze test results showed that oral administration of bajijiasu (35 mg/kg/day and 70 mg/kg/day) improved learning and memory abilities in APP/PS1 mice. Bajijiasu reduced ROS and MDA levels in both the hippocampus and cortex. Moreover, western blotting results showed that bajijiasu protected neurons from apoptosis, elevated the expression levels of neurotrophic factors, and alleviated endoplasmic reticulum stress in both the hippocampus and cortex. Conclusion: These results indicate that the mechanisms underlying the effects of bajijiasu on AD might be related to beta-amyloid-downstream pathologies, particularly endoplasmic reticulum stress.

scholarly journals An E3 Ubiquitin Ligase, Synoviolin, Is Involved in the Degradation of Homocysteine-Inducible Endoplasmic Reticulum Protein

2018 ◽  
Vol 41 (6) ◽  
pp. 915-919 ◽  
Author(s):  
Tomoji Maeda ◽  
Yu Fujita ◽  
Chiaki Tanabe-Fujimura ◽  
Kun Zou ◽  
Junjun Liu ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Endoplasmic Reticulum Protein

scholarly journals RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase

FEBS Letters ◽  
2012 ◽  
Vol 586 (16) ◽  
pp. 2488-2493 ◽  
Author(s):  
Maria Fairbank ◽  
Kun Huang ◽  
Alaa El-Husseini ◽  
Ivan R. Nabi
Keyword(s):  
Endoplasmic Reticulum ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger

scholarly journals The Heat Shock Protein 40-Type Chaperone MASH Supports the Endoplasmic Reticulum-Associated Degradation E3 Ubiquitin Ligase MAKIBISHI1 in Medicago truncatula

2021 ◽  
Vol 12 ◽  
Author(s):  
Marie-Laure Erffelinck ◽  
Bianca Ribeiro ◽  
Lore Gryffroy ◽  
Avanish Rai ◽  
Jacob Pollier ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Medicago Truncatula ◽  
Ubiquitin Ligase ◽  
Protein Quality ◽  
E3 Ubiquitin Ligase ◽  
Metabolic Phenotype ◽  
Endoplasmic Reticulum Associated Degradation ◽  
Control Apparatus

Jasmonates (JA) are oxylipin-derived phytohormones that trigger the production of specialized metabolites that often serve in defense against biotic stresses. In Medicago truncatula, a JA-induced endoplasmic reticulum-associated degradation (ERAD)-type machinery manages the production of bioactive triterpenes and thereby secures correct plant metabolism, growth, and development. This machinery involves the conserved RING membrane-anchor (RMA)-type E3 ubiquitin ligase MAKIBISHI1 (MKB1). Here, we discovered two additional members of this protein control apparatus via a yeast-based protein–protein interaction screen and characterized their function. First, a cognate E2 ubiquitin-conjugating enzyme was identified that interacts with MKB1 to deliver activated ubiquitin and to mediate its ubiquitination activity. Second, we identified a heat shock protein 40 (HSP40) that interacts with MKB1 to support its activity and was therefore designated MKB1-supporting HSP40 (MASH). MASH expression was found to be co-regulated with that of MKB1. The presence of MASH is critical for MKB1 and ERAD functioning because the dramatic morphological, transcriptional, and metabolic phenotype of MKB1 knock-down M. truncatula hairy roots was phenocopied by silencing of MASH. Interaction was also observed between the Arabidopsis thaliana (Arabidopsis) homologs of MASH and MKB1, suggesting that MASH represents an essential and plant-specific component of this vital and conserved eukaryotic protein quality control machinery.

scholarly journals The E3 Ubiquitin Ligase SYVN1 Ubiquitinates Atlastins to Remodel the Endoplasmic Reticulum Network

iScience ◽  
2020 ◽  
Vol 23 (9) ◽  
pp. 101494
Author(s):  
Yupeng Zhao ◽  
Zhigang Feng ◽  
Yan Zou ◽  
Yanfen Liu
Keyword(s):  
Endoplasmic Reticulum ◽  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase

A Novel Therapeutic Target Against Alzeimer's Disease: HRD1 as Endoplasmic Reticulum Stress-Related Ubiquitin Ligase

2014 ◽  
Vol 35 ◽  
pp. S17
Author(s):  
Yasuyuki Nomura ◽  
M. Kaneko ◽  
R. Saito ◽  
Y. Okuma ◽  
Y. Kitamura ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Ubiquitin Ligase ◽  
Therapeutic Target ◽  
Novel Therapeutic

scholarly journals Combined Neuroprotective Effects of Propofol and Dexmedetomidine on Endoplasmic Reticulum Stress-mediated Apoptosis in SH-SY5Y Cells

2016 ◽  
Vol 28 (3) ◽  
pp. 219-231
Author(s):  
Masayuki SOMEI ◽  
Manami INAGAKI ◽  
Tatsunori OGUCHI ◽  
Ran ONO ◽  
Mayumi TSUJI ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Neuroprotective Effects

scholarly journals Characterization of protein complexes of the endoplasmic reticulum-associated degradation E3 ubiquitin ligase Hrd1

2017 ◽  
Vol 292 (22) ◽  
pp. 9104-9116 ◽  
Author(s):  
Jiwon Hwang ◽  
Christopher P. Walczak ◽  
Thomas A. Shaler ◽  
James A. Olzmann ◽  
Lichao Zhang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Ubiquitin Ligase ◽  
Protein Complexes ◽  
E3 Ubiquitin Ligase ◽  
Endoplasmic Reticulum Associated Degradation
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