28
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Ghrelin octanoylation mediated by an orphan lipid transferase.

      Proceedings of the National Academy of Sciences of the United States of America

      Acylation, Acyltransferases, genetics, metabolism, Animals, Caprylates, Cell Line, Tumor, Cell Membrane, enzymology, Conserved Sequence, Gene Expression Profiling, Gene Expression Regulation, Enzymologic, Ghrelin, blood, Humans, Molecular Sequence Data, Pancreas, Peptides, RNA, Messenger, Serine, Stomach

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

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

          Related collections

          Author and article information

          Journal
          18443287
          2359796
          10.1073/pnas.0800708105

          Comments

          Comment on this article