This entry represents the RGS domain of SNX14 (Sorting Nexin14). RGS domain is a small α-helical structure that acts as GAPs for Galpha subunits of heterotrimeric G-proteins, and thus plays critical roles in attenuating G-protein coupled receptor (GPCR) signaling []. SNX14 is believed to regulate membrane trafficking in motor neurons []. It has been found localized to lysosomes and associated with phosphatidylinositol (3,5)-bisphosphate, a key component of late endosomes/lysosomes [].
SNX14 (sorting nexin-14) is expressed in the embryonic nervous system of mammals such as mice, being co-expressed with homoprotein islet-1 in several tissues []. SNX14 levels increase progressively during neuronal development and its knockdown impairs both excitatory and inhibitory synaptic transmission, suggesting a role in neuronal development and function []. SNX14 contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal PXC domain []. Its RGS domain is non-functional as a GTPase activator for Galpha, but it binds to and sequesters Galpha, thus inhibiting downstream cAMP production [].This entry represents the PX domain of SNX14. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions [, ].
