Journal
JOURNAL OF CELL BIOLOGY
Volume 148, Issue 5, Pages 915-924Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.148.5.915
Keywords
hydroxymethylglutaryl CoA reductase; Ca2+-transporting ATPase; ubiquitin; endoplasmic reticulum; Saccharomyces cerevisiae
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Funding
- NIDDK NIH HHS [DK5199601] Funding Source: Medline
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The integral ER membrane protein HMG-CoA reductase (HMGR) is a key enzyme of the mevalonate pathway from which sterols and other essential molecules are produced. HMGR degradation occurs in the ER and is regulated by mevalonate-derived signals. Little is known about the mechanisms responsible for regulating HMGR degradation. The yeast Hmg2p isozyme of HMGR undergoes regulated degradation in a manner very similar to mammalian HMGR, allowing us to isolate mutants deficient in regulating Hmg2p stability. We call these mutants con mutants for the control of HMG-CoA reductase degradation. With this screen, we have identified the first gene of this class, COD1, which encodes a P-type ATPase and is identical to SPF1. Our data suggested that Cod1p is a calcium transporter required for regulating Hmg2p degradation. This role for Cod1p is distinctly different from that of the well-characterized Ca2+ P-type ATPase Pmr1p which is neither required for Hmg2p degradation nor its control. The identification of Cod1p is especially intriguing in light of the role Ca2+ plays in the regulated degradation of mammalian HMGR.
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