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The GTP binding regulatory proteins (G proteins) consist of three subunits: α, β, and γ. These heterotrimeric proteins function at membranes to relay signals from cell surface receptors to intracellular effectors. The α subunit is unique for each G protein and contains the site of GTP binding and hydrolysis, as well sites for receptor and effector interactions. The βγ subunit complex interacts directly with receptors and the α subunit. The Gα family includes four families: the Gαs family including Gαs , Gαo1f, and Gαt, the Gαi family including Gαi, Gαo, and Gαz, the Gαq/Gα11 family and the Gα12/13 family. The Gαq protein is 88% homologus with Gα11 and both are widely expressed. These G proteins activate phospholipase C proteins, which induce calcium signaling events. G protein coupled receptors (GPCRs) involved in regulating Wnt signaling activate Gαq, phospholipase Cβ, and induce calcium-dependent activation of calpain. These events promote β-catenin nuclear export and proteolysis. Gαq has also been implicated in metabotropic glutamate receptor signaling. Thus, Gαq isoforms activate phospholipase C proteins in various G-protein coupled receptor pathways.Immunofluorescence, Western Blotting
