SREBPs: sterol-regulated transcription factors

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SREBPs: sterol-regulated transcription factors.

Studies of the feedback regulation of cholesterol synthesis in animals have led to the identification of a unique family of membrane-bound transcription factors, sterol regulatory element binding proteins (SREBPs) (Brown and Goldstein, 1997). In the presence of cholesterol, SREBPs are sequestered in the endoplasmic reticulum (ER). In the absence of a sterol signal, however, SREBPs undergo speci...

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Control of lipid metabolism by regulated intramembrane proteolysis of sterol regulatory element binding proteins (SREBPs).

In mammalian cells, the supply of lipids is co-ordinated with demand through the transcriptional control of genes encoding proteins required for synthesis or uptake. The sterol regulatory element binding proteins (SREBPs) are responsible for increased transcription of these genes when lipid level fall. Mammals have three SREBPs (-1a, -1c and -2), which are the products of two distinct genes. Sy...

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Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig.

Cholesterol synthesis in animals is controlled by the regulated transport of sterol regulatory element-binding proteins (SREBPs) from the endoplasmic reticulum to the Golgi, where the transcription factors are processed proteolytically to release active fragments. Transport is inhibited by either cholesterol or oxysterols, blocking cholesterol synthesis. Cholesterol acts by binding to the SREBP...

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Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: Insig renders sorting signal in Scap inaccessible to COPII proteins.

Two classes of sterols, cholesterol and oxysterols, block export of sterol regulatory element-binding proteins (SREBPs) from the endoplasmic reticulum (ER) to the Golgi by preventing the binding of COPII-coated proteins to a hexapeptide sorting signal (MELADL) in Scap, the SREBP-escort protein. Here, we show that anti-MELADL blocks COPII binding in vitro, and microinjection of Fab anti-MELADL b...

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Low-temperature effect on the sterol-dependent processing of SREBPs and transcription of related genes in HepG2 cells.

Lowering the growth temperature of HepG2 cells from 37 degrees C to 20 degrees C results in a 73% reduction in human squalene synthase (HSS) protein, a 76% reduction in HSS mRNA, and a 96% reduction in promoter activity of a secreted alkaline phosphatase-HSS reporter gene. A similar decrease in either mRNA or protein levels is observed for 3-hydroxy-3-methylglutaryl CoA reductase, farnesyl diph...

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ژورنال

عنوان ژورنال: Journal of Cell Science

سال: 2006

ISSN: 1477-9137,0021-9533

DOI: 10.1242/jcs.02866