Ghrelin receptor

More information on this family may be found on the IUPHAR-DB family and introduction pages.

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Ghrelin receptors [3] are activated by a 28 amino-acid peptide originally isolated from rat stomach, where it is cleaved from a 117 amino-acid precursor (ENSG00000157017). The human gene encoding the precursor peptide has 83% sequence homology to rat prepro-ghrelin, although the mature peptides from rat and human differ by only two amino acids [12]. Alternative splicing results in the formation of a second peptide, [des-Gln14]ghrelin with equipotent biological activity [9]. A unique post-translational modification (octanoylation of Ser3, catalysed by ghrelin Ο-acyltransferase [MBOAT4, ENSG00000177669], [15]) occurs in both peptides, essential for full activity in binding to the ghrelin receptors in the hypothalamus and pituitary; and the release of growth hormone release from the pituitary [11]. Structure activity studies showed the first five N-terminal amino acids to be the minimum required for binding [2], and receptor mutagenesis has indicated overlap of the ghrelin binding site with those for small molecule agonists and allosteric modulators of ghrelin function [7]. In cell systems, the ghrelin receptor is constitutively active [8], but this is abolished by a naturally occurring mutation (A204E) that results in decreased cell surface receptor expression and is associated with familial short stature [14].

Unless otherwise stated all data refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).

Receptors

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