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    Peptides. 2008 Jun;29(6):904-11. Epub 2008 Feb 13.

    Regulation of ghrelin structure and membrane binding by phosphorylation.

    Dehlin E, Liu J, Yun SH, Fox E, Snyder S, Gineste C, Willingham L, Geysen M, Gaylinn BD, Sando JJ.

    Source

    Department of Anesthesiology, University of Virginia, Charlottesville, VA 22908, United States.

    Abstract

    The peptide hormone ghrelin requires Ser-3 acylation for receptor binding, orexigenic and anti-inflammatory effects. Functions of desacylghrelin are less well understood. In vitro kinase assays reveal that the evolutionarily conserved Ser-18 in the basic C-terminus is an excellent substrate for protein kinase C. Circular dichroism reveals that desacylghrelin is approximately 12% helical in aqueous solution and approximately 50% helical in trifluoroethanol. Ser-18-phosphorylation, Ser-18-Ala substitution, or Ser-3-acylation reduces the helical character in trifluoroethanol to approximately 24%. Both ghrelin and desacylghrelin bind to phosphatidylcholine:phosphatidylserine sucrose-loaded vesicles in a phosphatidylserine-dependent manner. Phosphoghrelin and phosphodesacylghrelin show greatly diminished phosphatidylserine-dependent binding. These results are consistent with binding of ghrelin and desacylghrelin to acidic lipids via the basic face of an amphipathic helix with Ser-18 phosphorylation disrupting both helical character and membrane binding.

    PMID:
    18343535
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2413428
    Free PMC Article

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