Abstract
Abstract Robert D. Simoni began his foray into the world of lipids and membranes when he was in graduate school at the University of California, Davis, studying fatty lipid synthesis in plants with Paul Stumpf. Fewer than ten years later, Simoni started his own research program at Stanford University, exploring the biochemistry of cell membrane structure and function. The two Journal of Biological Chemistry (JBC) Classics articles reprinted here review some of Simoni's research on the regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase, which catalyzes the rate-limiting step in the synthesis of sterol and non-sterol isoprenoid products.
Highlights
hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR) is bound to the endoplasmic reticulum via an 8-membrane-spanning domain, whereas its catalytic domain resides in the cytosol (2)
The first Classics article shows that the enzyme’s increased degradation rate in response to sterols is dependent on its membrane anchor
Simoni and colleagues created a fusion construct consisting of the HMGR membrane domain and Escherichia coli -galactosidase
Summary
The Membrane Domain of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase Confers Endoplasmic Reticulum Localization and Sterol-regulated Degradation onto -Galactosidase Robert Dario Simoni was born in San Jose, California, in 1939. Simoni received a National Science Foundation postdoctoral fellowship, which he used to study membrane solute transport systems with JBC Classics author Saul Roseman (1) at The He rose through the ranks and eventually became the Donald Kennedy Chair in the School of Humanities and Sciences, a position he still holds today.
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