Redox-modulated SNX25 as a novel regulator of GPCR-G protein signaling from endosomes.

ABSTRACT: GPCR-G protein signaling from endosomes plays a crucial role in various physiological and pathological processes. However, the mechanism by which endosomal G protein signaling is terminated remains largely unknown. In this study, we aimed to investigate the regulatory mechanisms involved in terminating the signaling of Gα subunits from endosomes. Through structural analysis and cell-based assays, we have discovered that SNX25, a protein that targets endosomes via its PXA or PXC domain, interacts with regulator of G protein signaling (RGS) proteins (including RGS2, RGS4, RGS8, and RGS17) in a redox-regulated manner. The interaction between SNX25 and these RGS proteins enhances their GTPase-accelerating activity towards Gα_i/q and their ability to bind GDP-bound (inactive form) Gα<

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC11259961 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature