{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T06:48:03Z","timestamp":1790232483670,"version":"4.1.0"},"reference-count":36,"publisher":"Rockefeller University Press","issue":"5","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2000,3,6]]},"abstract":"<jats:p>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 cod 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.<\/jats:p>","DOI":"10.1083\/jcb.148.5.915","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:45:41Z","timestamp":1027701941000},"page":"915-924","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":92,"title":["Regulation of Hmg-Coa Reductase Degradation Requires the P-Type Atpase Cod1p\/Spf1p"],"prefix":"10.1083","volume":"148","author":[{"given":"Stephen R.","family":"Cronin","sequence":"first","affiliation":[{"name":"aDepartment of Biology, University of California San Diego, La Jolla, California, 92093-0347"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Afif","family":"Khoury","sequence":"additional","affiliation":[{"name":"aDepartment of Biology, University of California San Diego, La Jolla, California, 92093-0347"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dana K.","family":"Ferry","sequence":"additional","affiliation":[{"name":"aDepartment of Biology, University of California San Diego, La Jolla, California, 92093-0347"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Randolph Y.","family":"Hampton","sequence":"additional","affiliation":[{"name":"aDepartment of Biology, University of California San Diego, La Jolla, California, 92093-0347"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2000,3,6]]},"reference":[{"key":"2023072902135570700_AxelsenandPalmgren1998","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1007\/PL00006286","article-title":"Evolution of substrate specificities in the P-type ATPase superfamily","volume":"46","author":"Axelsen","year":"1998","journal-title":"J. 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