Eric Verdin, MD
Research Interests
My laboratory explores different aspects of the biology of reversible protein acetylation, a posttranslational modification that is gaining increasing recognition as an important biological regulatory mechanism. We focus on the enzymes that remove acetyl groups from proteins, the histone/protein deacetylases (HDACs). Of specific relevance to the liver are mitochondrial protein deacetylases. We have identified a mitochondrial protein deacetylase, SIRT3 and its first target, acetylcoenzyme A synthetase. We are currently identifying mitochondrial proteins that are acetylated, studying their regulation by SIRT3 and defining the role of protein acetylation in mitochondrial function and lipid metabolism.
Selected Publications
- Schwer B, Bunkenborg J, Verdin RO, Andersen JS, Verdin E. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc Natl Acad Sci U S A 2006;103:10224-10229.
- Lombard DB, Alt FW, Cheng HL, Bunkenborg J, Streeper RS, Mostoslavsky R, Kim J, Yancopoulos G, Valenzuela D, Murphy A, Yang Y, Chen Y, Hirschey M.D., Bronson RT, Haigis M, Guarente LP, Farese RV Jr, Weissman S, Verdin E, Schwer B. Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol Cell Biol 200727:8807-8814.
- Schwer B, Verdin E. Conserved metabolic regulatory functions of sirtuins. Cell Metab 2008;7:104-112.
- Professor
- Medicine
- Senior Investigator, Gladstone Institute of Virology and Immunology
Research Theme
- Hepatic Physiology and Metabolism
Contact Information
- everdin@
gladstone.ucsf.edu - Phone: (415) 734-4808
- Fax: (415) 355-0855
- 1650 Owens St.
- Box 1230, UCSF
- San Francisco, CA. 94158
Other UCSF Affiliations
- Gladstone Institute of Virology and Immunology
- BMS graduate program