Receptor selectivity between the G proteins Gα₁₂ and Gα₁₃ is defined by a single leucine-to-isoleucine variation.

ABSTRACT: Despite recent advances in structural definition of GPCR-G protein complexes, the basis of receptor selectivity between G proteins remains unclear. The Gα₁₂ and Gα₁₃ subtypes together form the least studied group of heterotrimeric G proteins. G protein-coupled receptor 35 (GPR35) has been suggested to couple efficiently to Gα₁₃ but weakly to Gα₁₂. Using combinations of cells genome-edited to not express G proteins and bioluminescence resonance energy transfer-based sensors, we confirmed marked selectivity of GPR35 for Gα₁₃. Incorporating Gα₁₂/Gα₁₃ chimeras and individual residue swap mutations into these sensors defined that selectivity between Gα₁₃ and Gα₁₂ was imbued largely by a single leu

SUBMITTER: Mackenzie AE 

PROVIDER: S-EPMC6436656 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature