RGS14 is a member of the regulator of G-protein signaling family which contains one RGS domain, two Raf-like Ras-binding domains (RBDs), and one GoLoco domain. RGS14 attenuates the signaling activity of G-proteins by binding, through its GoLoco domain, to specific types of activated, GTP-bound G alpha subunits. Acting as a GTPase activating protein (GAP), the protein increases the rate of conversion of the GTP to GDP. The resulting hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Alternate transcriptional splice variants of RGS14 have been observed but have not been thoroughly characterized. Further, RGS14 acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism; plays a role in cell division; is required for the nerve growth factor (NGF)-mediated neurite outgrowth, and is involved in stress resistance. RGS14 protein may also be involved in visual memory processing capacity and hippocampal-based learning and memory.
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Protein Aliases: rap1/rap2 interacting protein; RAP1/RAP2-interacting protein; Regulator of G-protein signaling 14; regulator of G-protein signalling 14; RGS14; RGSE; RPIP1
Gene Aliases: RGS14; RPIP1