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An intact helical domain is required for G14 to stimulate phospholipase C.

Kwan, DH;Wong, KM;Chan, AS;Yung, LY;Wong, YH;

Stimulation of phospholipase C (PLC) by the activated -subunit of Gq (Gq) constitutes a major signaling pathway for cellular regulation, and structural studies have recently revealed the molecular interactions between PLC and Gq. Yet, most of the PLC-interacting residues identified on Gq are not unique to members of the Gq family. Molecular modeling predicts that the core PLC-interacting residues located on the switch regions of Gq are similarly positioned in Gz which does not stimulate PLC. Using wild-type and constitutively active chimeras constructed between Gz and G14, a member of the Gq family, we examined if the PLC-interacting residues identified in Gq are indeed essential.