Abstract
Protein palmitoylation is a widespread lipid modification in which one or more cysteine thiols on a substrate protein are modified to form a thioester with a palmitoyl group. This lipid modification is readily reversible; a feature of protein palmitoylation that allows for rapid regulation of the function of many cellular proteins. Mutations in palmitoyltransferases (PATs), the enzymes that catalyze the formation of this modification, are associated with a number of neurological diseases and cancer progression. This review summarizes the crucial role of palmitoylation in biological systems, the discovery of the DHHC protein family that catalyzes protein palmitoylation, and the development of methods for investigating the catalytic mechanism of PATs.
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FIERKE Carol received her Ph.D. from the Department of Biochemstry (1984), Brandeis University. She was an NIH postdoctoral fellow at The Pennsylvania State University for three years and began her independent research career in the Biochemistry Department at Duke University Medical School where she was promoted to Associate Professor. She moved to the Chemistry Department at the University of Michigan in 1999 where she is now Department Chair and the Jerome and Isabella Karle Collegiate Professor of Chemistry and Professor of Biological Chemistry. Her research focuses on the mechanism of medically important enzymes. (photo by D.C. Goings).
GUAN XiaoMu graduated with a Chemistry B.S. degree from Peking University in 2006. She received her Ph.D. degree in Chemical Biology in 2011 with Professor Fierke at the University of Michigan. Her Ph.D. research focuses on characterizing the catalytic mechanism of yeast palmitoyltransferase Akr1p and the substrate selectivity of protein farnesyltransferase.
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Guan, X., Fierke, C.A. Understanding protein palmitoylation: Biological significance and enzymology. Sci. China Chem. 54, 1888–1897 (2011). https://doi.org/10.1007/s11426-011-4428-2
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DOI: https://doi.org/10.1007/s11426-011-4428-2