The GTP binding G (transglutaminase II) mediates the -adrenoreceptor signal to a 69-kDa phospholipase C (PLC). Thus, G possesses both GTPase and transglutaminase activities with a signal transfer role. The recognition sites of this unique GTP binding protein for either the receptor or the effector are completely unknown. A site on human heart G (hhG) has been identified that interacts with and stimulates PLC. Expressed mutants of hhG with deleted C-terminal regions lost the response to(-)-epinephrine and GTP and failed to coimmunoprecipitate PLC by the specific G antibody. The interaction regions were further defined by studies with synthetic peptides of hhG and a chimera in which residues Val-Lys of hhG were substituted with Ile-Ser residues of human coagulation factor XIIIa. Thus, eight amino acid residues near the C terminus of hhG are critical for recognition and stimulation of PLC.

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