Regulator of G-protein signaling 7-binding protein (RGS7BP)

Regulator of G-protein signaling 7-binding protein (RGS7BP) is a membrane-anchoring regulatory protein that controls the localization and function of the R7 subfamily of Regulator of G-protein Signaling (RGS) proteins (RGS6, RGS7, RGS9, RGS11), especially in neuronal signaling and sensory pathways. It acts as a critical membrane anchor and regulatory subunit for R7-RGS/Gβ5 complexes, guiding them to the plasma membrane through reversible palmitoylation. This enhances their ability to accelerate GTPase activity of certain Gα proteins, thereby modulating GPCR signaling. RGS7BP also protects R7 proteins from degradation. It is a critical master regulator for both acute and chronic itch sensation; knockout or inhibition of RGS7BP significantly reduces pruritic responses in animal models without apparent developmental effects. RGS7BP’s reversible localization between the membrane and nucleus enables dynamic control over sensory signal processing. Genetic variation in RGS7BP has been linked to neuropsychiatric and sensory disorders and may contribute to disease susceptibility, though no marketed drugs specifically target RGS7BP. Structural studies suggest RGS7BP interacts through defined grooves at the R7-RGS/Gβ5 interface and has differential binding affinities to specific RGS/Gβ5 complexes, opening possibilities for precise therapeutic targeting.

Other names

RGS7BPRegulator of G protein signaling 7 binding proteinR7BPR7 family-binding proteinRegulator of G-protein signaling 7-binding protein

Experimental antibody inhibitors block RGS7BP’s interaction with RGS7/Gβ5, thus modulating sensory signaling pathways (e.g., itch).