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J Biol Chem, Vol. 274, Issue 9, 5285-5291, February 26, 1999
From the Department of Molecular Biology and Biochemistry,
University of California, Irvine California 92697-3900
3-Hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
synthase, a key regulatory enzyme in the pathway for endogenous
cholesterol synthesis, is a target for negative feedback regulation by
cholesterol. When cellular sterol levels are low, the sterol regulatory
element-binding proteins (SREBPs) are released from the endoplasmic
reticulum membrane, allowing them to translocate to the nucleus and
activate SREBP target genes. However, in all SREBP-regulated promoters studied to date, additional co-regulatory transcription factors are
required for sterol-regulated activation of transcription. We have
previously shown that, in addition to SREBPs, NF-Y/CBF is required for
sterol-regulated transcription of HMG-CoA synthase. This heterotrimeric
transcription factor has recently been shown to function as a
co-regulator in several other SREBP-regulated promoters, as well. In
addition to cis-acting sites for both SREBP and NF-Y/CBF, the sterol
regulatory region of the synthase promoter also contains a consensus
cAMP response element (CRE), an element that binds members of the
CREB/ATF family of transcription factors. Here, we show that this
consensus CRE is essential for sterol-regulated transcription of the
synthase promoter. Using in vitro binding assays, we also
demonstrate that CREB binds to this CRE, and mutations within the CRE
that result in a loss of CREB binding also result in a loss of
sterol-regulated transcription. We further show that efficient
activation of the synthase promoter in Drosophila SL2 cells
requires the simultaneous expression of all three factors: SREBPs,
NF-Y/CBF, and CREB. To date this is the first promoter shown to require
CREB for efficient sterol-regulated transcription, and to require two
different co-regulatory factors in addition to SREBPs for maximal activation.
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