Physiology of RGS10 in Neurons and Immune Cells.

Abstract

Regulator of G protein signaling-10 (RGS10), a GTPase-activating protein (GAP) for Gαi3, Gαq, and Gαz, belongs to the D/R12 subfamily based on the homology within the RGS domain and is one of the smallest RGS proteins, outside the RGS box. Although RGS10 lacks the flanking domains or motifs, RGS10 can be targeted to membrane by palmitoylation which markedly increases its net GAP activity. The cAMP-dependent protein kinase A phosphorylates RGS10 on serine 168 (Ser(168)) which promotes translocation of RGS10 from the cytosol to nucleus. In addition to its GAP function, RGS10 modulates adenylyl cyclase (AC) activity as well as the G protein-gated inwardly rectifying potassium channels. Although the roles of various RGS proteins have been well addressed in previous reviews, the function and mechanism of RGS10 in particular has not been reviewed in-depth. Moreover, recent arrays of studies implicate a role for RGS10 in immune and neuronal cells. RGS10 has been localized to various cell compartments including the cytoplasm and nucleus. In this chapter, we will review its role in neurons and immune cells.