New dimensions in G protein signalling: G beta 5 and the RGS proteins.

ABSTRACT

The beta gamma complex of G-proteins regulates effectors independently of the G alpha subunits, such that upon activation G proteins give may signal downstream along one or both pathways. The G beta 5 isoform exhibits much less homology with other G beta isoforms (approximately 50%) and is preferentially expressed in brain. The G beta 5 isoform exhibits novel properties in its activation of effector pathways such as MAPK, phospholipase C-beta, and adenylyl cyclase type II when compared to G beta 1. Recently specific native complexes between G beta 5 and the regulator of G protein signaling (RGS) protein-7 (RGS7) and between G beta 5L (a splice variant with a 42 amino acid N-terminal extension) and RGS9 have been isolated from different retinal fractions. Such findings are not accounted for by current models as only the G alpha subunits and not G beta had been previously implicated in RGS protein function. These recent novel observations further reinforce the view of G beta 5 as a unique and highly specialized G protein subunit.