Ghrelin octanoylation mediated by an orphan lipid transferase

• DOI: 10.1073/pnas.0800708105
• Publication Date: 2008-04-29T01:26:54Z
• Authors: Jesus A. Gutierrez; Patricia J. Solen...; Douglas R. Perkins; Jill A. Willency; Michael D. Knierman; Zhaoyan Jin; Derrick R. Witcher; Shuang Luo; Jude E. Onyia; John E. Hale
• Keywords: Obestatin; Transferase

The peptide hormone ghrelin is the only known protein modified with an O-linked octanoyl side group, which occurs on its third serine residue. This modification crucial for ghrelin's physiological effects including regulation of feeding, adiposity, and insulin secretion. Despite role octanoylation in physiology ghrelin, lipid transferase that mediates this novel has remained unknown. Here we report identification characterization human GOAT, O-acyl transferase. GOAT a conserved orphan membrane-bound (MBOAT) specifically octanoylates serine-3 peptide. Transcripts both occur predominantly stomach pancreas. across vertebrates, genetic disruption gene mice leads to complete absence acylated circulation. occurrence pancreas tissues demonstrates relevance acylation further implicates pancreatic function.