The Gαi protein subclass selectivity to the dopamine D₂ receptor is also decided by their location at the cell membrane.

ABSTRACT:

Background

G protein-coupled receptor (GPCR) signaling via heterotrimeric G proteins plays an important role in the cellular regulation of responses to external stimuli. Despite intensive structural research, the mechanism underlying the receptor-G protein coupling of closely related subtypes of Gαi remains unclear. In addition to the structural changes of interacting proteins, the interactions between lipids and proteins seem to be crucial in GPCR-dependent cell signaling due to their functional organization in specific membrane domains. In previous works, we found that Gαs and Gαi₃ subunits prefer distinct types of membrane-anchor lipid domains that also modulate the G protein trimer localization. In the present study, we investigated the functional selectivity of dopa

SUBMITTER: Polit A 

PROVIDER: S-EPMC7731117 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature