Eukaryotic G protein signaling evolved to require G protein-coupled receptors for activation.

ABSTRACT: Although bioinformatic analysis of the increasing numbers of diverse genome sequences and amount of functional data has provided insight into the evolution of signaling networks, bioinformatics approaches have limited application for understanding the evolution of highly divergent protein families. We used biochemical analyses to determine the in vitro properties of selected divergent components of the heterotrimeric guanine nucleotide-binding protein (G protein) signaling network to investigate signaling network evolution. In animals, G proteins are activated by cell-surface seven-transmembrane (7TM) receptors, which are named G protein-coupled receptors (GPCRs) and function as guanine nucleotide exchange factors (GEFs). In contrast, the plant G protein is intrinsically active, and a 7TM

SUBMITTER: Bradford W 

PROVIDER: S-EPMC4871593 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature