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J Biol Chem, Vol. 274, Issue 44, 31671-31678, October 29, 1999
From the Department of Biology, University of California, San
Diego, La Jolla, California 92093
Sterol synthesis by the mevalonate pathway is
modulated, in part, through feedback-regulated degradation of
3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR). In both mammals
and yeast, a non-sterol isoprenoid signal positively regulates the rate
of HMGR degradation. To define more precisely the molecule that serves
as the source of this signal, we have conducted both pharmacological
and genetic manipulations of the mevalonate pathway in yeast. We now
demonstrate that farnesyl diphosphate (FPP) is the source of the
positive signal for Hmg2p degradation in yeast. This FPP-derived signal
does not act by altering the endoplasmic reticulum degradation
machinery in general. Rather, the FPP-derived signal specifically
modulates Hmg2p stability. In mammalian cells, an FPP-derived molecule
also serves as a positive signal for HMGR degradation. Thus, both yeast
and mammalian cells employ the same strategy for regulation of HMGR
degradation, perhaps by conserved molecular processes.
A Highly Conserved Signal Controls Degradation of
3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) Reductase in
Eukaryotes
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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