RGS10 is a GTPase-activating protein that negatively regulates G protein-coupled receptor (GPCR) signaling by accelerating GTPase activity of Gαi3, Gαq, and Gαz subunits, converting them to their inactive GDP-bound state 1. Beyond its core GAP function, RGS10 modulates adenylyl cyclase activity and G protein-gated inwardly rectifying potassium channels 1. Its subcellular localization is dynamic: palmitoylation targets RGS10 to membranes to enhance GAP activity, while PKA-mediated phosphorylation at serine 168 promotes nuclear translocation 1. RGS10 plays critical roles in immune homeostasis and platelet regulation. It attenuates systemic immune dysregulation during chr10 inflammatory stress by suppressing inflammatory and cytotoxic cell populations 2. RGS10 levels are reduced in Parkinson's disease patients' cerebrospinal fluid and peripheral immune cells 2. In platelets, RGS10 and RGS18 have complementary roles limiting activation, promoting production, and prolonging survival 3. Notably, RGS10 deficiency alleviates ulcerative colitis through suppression of Th1/Th17 differentiation via interaction with PTPN2 4. In cancer, RGS10 expression is epigenetically suppressed in chemoresistant ovarian cancer through DNA hypermethylation and histone deacetylation 56. Restoring RGS10 expression enhances cisplatin sensitivity 6. Human RGS10 mutations cause immunodeficiency and short stature due to altered protein localization and aberrant chemokine signaling 7.