RGS17 weakens the signaling activity of G-proteins by binding to activated GTP-bound G alpha subunits and performing as a GTPase activating protein （GAP）， increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers， creating inactive G-protein heterotrimers， which terminates the signal. RGS17 has a vital part in ending the signaling by mu opioid receptors and development of tolerance to opioid analgesic drugs.
