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Sterol regulatory element binding protein-2 (SREBP-2) is a membrane-bound transcription factor that upon proteolytic processing can activate the expression of genes involved in cholesterol biosynthesis and uptake. We as well as others have demonstrated that the accumulation of misfolded proteins within the endoplasmic reticulum (ER), a condition known as ER stress, can dysregulate lipid metabolism by activating the SREBPs. The purpose of this study was to determine the mechanism by which ER stress induces SREBP-2 activation.

HeLa and MCF7 cells were treated with ER stress-inducing agents to determine the effect of ER stress on SREBP-2 cleavage and subsequent cholesterol accumulation. Cells treated with thapsigargin (Tg) exhibit proteolytic cleavage of SREBP-2. Proteolytic cleavage of SREBP-2 induced by Tg occurred independently of caspase …