The regulator of G protein signaling 10 (RGS10) protein is a regulatory molecule that belongs to a larger family of RGS proteins responsible for altering cellular signaling. Generally, RGS proteins are negative regulators of signal transduction pathways mediated by heterotrimeric G proteins. This function allows RGS proteins to control the duration and amplification of signaling activity, ultimately operating as shut-off switches. RGS proteins deactivate G protein subunits by serving as GTPase activating proteins (GAPs), which enhance the intrinsic GTPase activity of the active, GTP-bound Gα subunit and return G proteins to their inactive, GDP-bound form. The result is an acceleration of the deactivation of G protein signaling.
Protein Structure and Function
All RGS proteins share a conserved 120 amino acid helical RGS domain that is responsible for GAP activity. Based on sequence similarity of the RGS domain, RGS10 is grouped in the RGS 12 subfamily which also...
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