Heterotrimeric guanine nucleotide-binding proteins (G proteins) consist of alpha, beta and gamma subunits and mediate the effects of hormones, neurotransmitters, chemokines and sensory stimuli. To date, over 20 known Galpha subunits have been classified into four families, Galpha(s), Galpha(i/o), Galpha(q) and Galpha(12), based on structural and functional similarities (1,2). Phosphorylation of Tyr356 of Galpha(q)/Galpha(11) is essential for activation of the G protein, since phenylalanine substitution for Tyr356 changes the interaction of Galpha with receptors and abolishes ligand-induced IP3 formation (3).
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