Russell DeBose-Boyd, Ph. D. is the Beatrice and Miguel Elias Distinguished Chair in Biomedical Science and Professor of Molecular Genetics at the University of Texas Southwestern Medical Center in Dallas, TX. He earned his B.S. in Chemistry from Southeastern Oklahoma State University and his Ph.D. in Biochemistry and Molecular Biology from the University of Oklahoma Health Sciences Center. Dr. DeBose-Boyd joined the laboratory of Joseph L. Goldstein, M.D. and Michael S. Brown, M.D. at the University of Texas Southwestern Medical Center as a postdoctoral fellow and joined the Department of Molecular Genetics faculty in 2003. He has been named an Established Investigator of the American Heart Association, a W.M. Keck Distinguished Young Scholar in Medical Research, and a Howard Hughes Medical Institute Early Career Scientist. Dr. DeBose-Boyd’s awards include the Jane Coffin Childs Memorial Postdoctoral Fellowship, David L. Williams Memorial Lectureship Award, John J. Abel Award in Pharmacology, DeWitt Goodman Lectureship Award, Edward Bierman Award from the American Diabetes Association, David S. Sigman Lectureship Award, and the Avanti Award in Lipids. In 2023, Dr. DeBose-Boyd was elected to the United States National Academy of Sciences.

Research Interests

Endoplasmic reticulum (ER)-localized HMG CoA reductase (HMGCR) produces mevalonate, a key intermediate in synthesis of cholesterol and nonsterol isoprenoids including farnesyl pyrophosphate, geranylgeranyl pyrophosphate (GGpp), ubiquinone-10, and dolichol. Dr. DeBose-Boyd’s research focuses on one mechanism for feedback control of HMGCR involving sterol-induced ubiquitination, which marks the enzyme for ER-associated degradation (ERAD) that is augmented by GGpp. Intracellular accumulation of sterols causes HMGCR to bind ER membrane proteins called Insigs. Ubiquitination by Insig-associated ubiquitin ligases marks HMGCR for extraction across ER membranes and proteasome-mediated ERAD. Sterols also stimulate binding of HMGCR to UbiA prenyltransferase domain-containing protein-1 (UBIAD1), which utilizes GGpp to synthesize subtype of vitamin K. Binding to UBIAD1 protects HMGCR from ERAD, permitting continued synthesis of nonsterol isoprenoids even when sterols are abundant. GGpp triggers release of UBIAD1 from HMGCR, which enhances ERAD and triggers transport of UBIAD1 from the ER to Golgi. Missense mutations in UBIAD1 cause Schnyder corneal dystrophy (SCD), an autosomal dominant eye disease characterized by corneal accumulation of cholesterol. SCD-associated UBIAD1 resists GGpp-induced release from HMGCR and remains sequestered in the ER to inhibit ERAD, which leads to enhanced synthesis and intracellular accumulation of cholesterol.

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Primary Section

Section 42: Medical Physiology and Metabolism

Secondary Section

Section 21: Biochemistry