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Journal of Lipid Research, Vol 38, 1630-1638, Copyright © 1997 by Lipid Research, Inc.
MM Magana, SS Lin, KA Dooley and TF Osborne
The sterol regulatory element binding proteins (SREBPs) are central
regulators of lipid homeostasis in mammalian cells. Their activity is
controlled by a sterol-regulated two-step proteolytic process that releases
the nuclear targeted amino-terminal domain from the membrane anchored
carboxyl-terminal remnant. This ensures that transcriptional stimulation of
the appropriate genes occurs only when increased intracellular sterol
accumulation is required. Gene targets for SREBP encode key proteins of
cholesterol metabolism as well as essential proteins of fatty acid
biosynthesis, providing a mechanism for coordinate control of these two
major lipid pathways when sterols and fatty acids need to accumulate
together. However, the regulatory mechanism must provide a way to uncouple
these two pathways to allow separate regulation when sterol or fat levels
need to increase independently of each other. We compared the similarities
and differences for how SREBP activates the promoter for the low density
lipoprotein (LDL) receptor, which is the key protein involved in
cholesterol uptake, relative to how it activates promoters for acetyl
coenzyme A carboxylase (ACC) and fatty acid synthase (FAS), which are both
key enzymes of fatty acid biosynthesis. In the current studies we show
there are two distinct sites for SREBP binding that control activation of
the ACC PII promoter whereas previous work has shown there is only a single
SREBP site in the LDL receptor. Additionally, disruption of either ACC site
results in a total loss in promoter function and a severe decrease in SREBP
binding even to the neighboring unaltered site. Thus, the two sites are
equally important and dependent on one another for optimal function. This
is in contrast to the FAS promoter where SREBP binds to two adjacent sites
independently and the one located closer to the binding site for the Sp1
co-regulator is more critical for sterol regulation and activation by SREBP
over-expression.
ARTICLES
Sterol regulation of acetyl coenzyme A carboxylase promoter requires two interdependent binding sites for sterol regulatory element binding proteins
Department of Molecular Biology and Biochemistry, University of California, Irvine 92697-3900, USA.
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