Sterol regulatory element-binding proteins: transcriptional activators of lipid synthesis

2002 ◽  
Vol 30 (6) ◽  
pp. 1091-1095 ◽  
Author(s):  
J. D. Horton

Sterol regulatory element-binding proteins (SREBPs) are a family of transcription factors that regulate lipid homoeostasis. Three SREBP iso-forms control the expression of more than 30 genes required for the biosynthesis of cholesterol, fatty acids, triacylglycerols and phospholipids. The unique regulation and activation properties of each SREBP isoform facilitates the co-ordinate regulation of all essential lipid building blocks required for cell membranes as well as for very-low-density lipoprotein formation in hepatocytes.

2019 ◽  
Vol 26 (1) ◽  
Author(s):  
Gang Chen ◽  
Xuemei Li

Abstract Dysregulated lipid profile with hypertriglyceridemia and increased low-density lipoprotein (LDL) is common in chronic kidney disease (CKD) whereas the reason is unclear. A similar phenomenon is found in the elder population. Silent information regulator-1 (SIRT1) associates with many modulators regulating lipid metabolism and results in increased expression of sterol regulatory element-binding proteins (SREBPs), which functions as a key modulator in lipid synthesis. Since CKD is being viewed as a premature aging model and SIRT1 is known to decrease during the process of aging, we hypothesize that SIRT1 level is reduced in the liver when CKD develops and eventually result in dysregulated lipid profile.


Contact ◽  
2020 ◽  
Vol 3 ◽  
pp. 251525642093467
Author(s):  
Zhe Cao ◽  
Ho Yi Mak

The endoplasmic reticulum (ER) is a hub that coordinates neutral lipid synthesis, storage, and export. To fulfill this role, the ER maintains close contact with lipid droplets (LDs), which are evolutionarily conserved organelles for the storage of neutral lipids. Decades of biochemical evidence points to fatty acid modification and neutral lipid synthesis in the ER. Conceptually, lipid export into extracellular space or lipid retention intracellularly require the subsequent remodeling of an ER membrane leaflet that faces the lumen or cytoplasm, respectively. This is because LDs and very-low-density lipoprotein particles are all structures surrounded by a phospholipid monolayer. While the export of neutral lipids via very-low-density lipoprotein production is well characterized, there has been increasing interest in the mechanisms that underlie neutral lipid retention in LDs. Structural determination, in vitro reconstitution, and localization of key proteins by advanced microscopy techniques collectively enrich models of ER-LD engagement. In this review, we consider current concepts on how LDs emerge from the ER in a directional manner and how sustained ER-LD contacts support LD expansion.


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