Endogenous l- to d-amino acid residue isomerization modulates selectivity between distinct neuropeptide receptor family members.

ABSTRACT: The l- to d-amino acid residue isomerization of neuropeptides is an understudied post-translational modification found in animals across several phyla. Despite its physiological importance, little information is available regarding the impact of endogenous peptide isomerization on receptor recognition and activation. As a result, the full roles peptide isomerization play in biology are not well understood. Here, we identify that the Aplysia allatotropin-related peptide (ATRP) signaling system utilizes l- to d-residue isomerization of one amino acid residue in the neuropeptide ligand to modulate selectivity between two distinct G protein-coupled receptors (GPCRs). We first identified a novel receptor for ATRP that is selective for the D2-ATRP form, which bears a single d-phenylalanin

SUBMITTER: Yussif BM 

PROVIDER: S-EPMC10089201 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature