C-terminal motif of human neuropeptide Y₄ receptor determines internalization and arrestin recruitment.

ABSTRACT: The human neuropeptide Y₄ receptor is a rhodopsin-like G protein-coupled receptor (GPCR), which contributes to anorexigenic signals. Thus, this receptor is a highly interesting target for metabolic diseases. As GPCR internalization and trafficking affect receptor signaling and vice versa, we aimed to investigate the molecular mechanism of hY₄R desensitization and endocytosis. The role of distinct segments of the hY₄R carboxyl terminus was investigated by fluorescence microscopy, binding assays, inositol turnover experiments and bioluminescence resonance energy transfer assays to examine the internalization behavior of hY₄R and its interaction with arrestin-3. Based on results of C-terminal deletion mutants and substitution of single amino acids,

SUBMITTER: Wanka L 

PROVIDER: S-EPMC5797669 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature