scholarly journals Emodin ameliorates hepatic steatosis through endoplasmic reticulum-stress sterol regulatory element-binding protein 1c pathway in liquid fructose-feeding rats

2015 ◽  
Vol 46 (3) ◽  
pp. E105-E117 ◽  
Author(s):  
Xiaojie Li ◽  
Zhimeng Xu ◽  
Shaojie Wang ◽  
Hongli Guo ◽  
Sizhe Dong ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Hepatic Steatosis ◽  
Binding Protein ◽  
Regulatory Element ◽  
Element Binding Protein ◽  
Sterol Regulatory Element

SREBP-1c and lipogenesis in the liver: an update

2021 ◽  
Vol 478 (20) ◽  
pp. 3723-3739
Author(s):  
Pascal Ferré ◽  
Franck Phan ◽  
Fabienne Foufelle
Keyword(s):  
Endoplasmic Reticulum ◽  
Transcription Factor ◽  
Endoplasmic Reticulum Stress ◽  
Binding Protein ◽  
Regulatory Element ◽  
Activation Process ◽  
Lipogenic Genes ◽  
Regulated Intramembrane Proteolysis ◽  
Element Binding Protein ◽  
Sterol Regulatory Element

Sterol Regulatory Element Binding Protein-1c is a transcription factor that controls the synthesis of lipids from glucose in the liver, a process which is of utmost importance for the storage of energy. Discovered in the early nineties by B. Spiegelman and by M. Brown and J. Goldstein, it has generated more than 5000 studies in order to elucidate its mechanism of activation and its role in physiology and pathology. Synthetized as a precursor found in the membranes of the endoplasmic reticulum, it has to be exported to the Golgi and cleaved by a mechanism called regulated intramembrane proteolysis. We reviewed in 2002 its main characteristics, its activation process and its role in the regulation of hepatic glycolytic and lipogenic genes. We particularly emphasized that Sterol Regulatory Element Binding Protein-1c is the mediator of insulin effects on these genes. In the present review, we would like to update these informations and focus on the response to insulin and to another actor in Sterol Regulatory Element Binding Protein-1c activation, the endoplasmic reticulum stress.

scholarly journals Subunit Architecture of the Golgi Dsc E3 Ligase Required for Sterol Regulatory Element-binding Protein (SREBP) Cleavage in Fission Yeast

2013 ◽  
Vol 288 (29) ◽  
pp. 21043-21054 ◽  
Author(s):  
S. Julie-Ann Lloyd ◽  
Sumana Raychaudhuri ◽  
Peter J. Espenshade
Keyword(s):  
Endoplasmic Reticulum ◽  
Fission Yeast ◽  
Binding Protein ◽  
Regulatory Element ◽  
E3 Ligase ◽  
E3 Ligases ◽  
Endoplasmic Reticulum Associated Degradation ◽  
Element Binding Protein ◽  
Uba Domain ◽  
Sterol Regulatory Element

The membrane-bound sterol regulatory element-binding protein (SREBP) transcription factors regulate lipogenesis in mammalian cells and are activated through sequential cleavage by the Golgi-localized Site-1 and Site-2 proteases. The mechanism of fission yeast SREBP cleavage is less well defined and, in contrast, requires the Golgi-localized Dsc E3 ligase complex. The Dsc E3 ligase consists of five integral membrane subunits, Dsc1 through Dsc5, and resembles membrane E3 ligases that function in endoplasmic reticulum-associated degradation. Using immunoprecipitation assays and blue native electrophoresis, we determined the subunit architecture for the complex of Dsc1 through Dsc5, showing that the Dsc proteins form subcomplexes and display defined connectivity. Dsc2 is a rhomboid pseudoprotease family member homologous to mammalian UBAC2 and a central component of the Dsc E3 ligase. We identified conservation in the architecture of the Dsc E3 ligase and the multisubunit E3 ligase gp78 in mammals. Specifically, Dsc1-Dsc2-Dsc5 forms a complex resembling gp78-UBAC2-UBXD8. Further characterization of Dsc2 revealed that its C-terminal UBA domain can bind to ubiquitin chains but that the Dsc2 UBA domain is not essential for yeast SREBP cleavage. Based on the ability of rhomboid superfamily members to bind transmembrane proteins, we speculate that Dsc2 functions in SREBP recognition and binding. Homologs of Dsc1 through Dsc4 are required for SREBP cleavage and virulence in the human opportunistic pathogen Aspergillus fumigatus. Thus, these studies advance our organizational understanding of multisubunit E3 ligases involved in endoplasmic reticulum-associated degradation and fungal pathogenesis.

scholarly journals RETRACTED: Reversion of hepatic steatosis by exercise training in obese mice: The role of sterol regulatory element-binding protein-1c

Life Sciences ◽  
2012 ◽  
Vol 91 (11-12) ◽  
pp. 395-401 ◽  
Author(s):  
Dennys E. Cintra ◽  
Eduardo R. Ropelle ◽  
Marcelo F. Vitto ◽  
Thais F. Luciano ◽  
Daniela R. Souza ◽  
...  
Keyword(s):  
Exercise Training ◽  
Hepatic Steatosis ◽  
Binding Protein ◽  
Regulatory Element ◽  
Obese Mice ◽  
Element Binding Protein ◽  
Sterol Regulatory Element
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