RGS17 contains a conserved 120 amino acid motif known as the RGS domain and a cysteine-rich region . The primary function of RGS17 is to attenuate the signaling activity of G-proteins by binding to activated, GTP-bound G alpha subunits. It acts as a GTPase-activating protein (GAP), increasing the rate of conversion of GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers and thereby terminating the signal .
RGS17 is typically expressed in the human central nervous system but is also found in other tissues such as the buccal mucosa, tendon of biceps brachii, cartilage tissue, and pancreatic ductal cells . It is involved in various cellular components, including the cytoplasm, neuron projection, cell junction, synapse, membrane, nucleus, and cytoplasmic vesicle .
RGS17 has been identified as a putative lung cancer susceptibility gene located on chromosome 6q in humans . It is overexpressed in lung and prostate cancers and is required for the maintenance of proliferation in lung tumor cell lines . Additionally, RGS17 plays a role in the termination of signaling by mu opioid receptors and the development of tolerance to opioid analgesic drugs .
RGS17 has been extensively studied for its role in inhibiting μ-opioid, dopamine, and cannabinoid receptors in the central nervous system . An interesting function of RGS17 is its potential role as a redox transducer, mediated by the interaction of its cysteine-rich domain with nitric oxide to release zinc . This makes RGS17 a novel target for therapeutic interventions in various diseases, including cancer and neurological disorders .