Disentangling autoproteolytic cleavage from tethered agonist-dependent activation of the adhesion receptor ADGRL3.

ABSTRACT: Adhesion G protein-coupled receptor latrophilin 3 (ADGRL3), a cell adhesion molecule highly expressed in the central nervous system, acts in synapse formation through trans interactions with its ligands. It is largely unknown if these interactions serve a purely adhesive function or can modulate G protein signaling. To assess how different structural elements of ADGRL3 (e.g., the adhesive domains, autoproteolytic cleavage site, or tethered agonist (TA)) impact receptor function, we require constructs that disrupt specific receptor features without impacting others. While we showed previously that mutating conserved Phe and Met residues in the TA of ADGRL3-C-terminal fragment (CTF), a CTF truncated to the G protein-coupled receptor proteolysis site, abolishes receptor-mediated G protein act

SUBMITTER: Perry-Hauser NA 

PROVIDER: S-EPMC9674912 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature