Differential Role of Phosphorylation in Glucagon Family Receptor Signaling Revealed by Mass Spectrometry.

ABSTRACT: In response to extracellular ligands, G protein-coupled receptors (GPCRs) undergo conformational changes that induce coupling to intracellular effectors such as heterotrimeric G proteins that trigger various downstream signaling pathways. These events have been shown to be highly regulated by concerted effects of post-translational modifications (PTMs) that occur in a ligand-dependent manner. Most notably, phosphorylation of residues in the C-terminal cytoplasmic tail of GPCRs has been strongly implicated in promoting receptor interactions with β-arrestins (βarrs), which are cytosolic adaptor proteins that modulate G protein coupling, receptor internalization, and perhaps also serve as signaling modules in their own right. Here, we use proteomic methods to identify C-tail residues that are

SUBMITTER: Lamb IM 

PROVIDER: S-EPMC12235690 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature