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. 2016 Apr;89(4):407–412. doi: 10.1124/mol.115.101626

Fig. 4.

Fig. 4.

Gαs stimulates SYNAC synergistically with FSK in a GTP-dependent manner. (A) FSK and Gαs synergistically stimulate SYNAC in a GTP-dependent manner. SYNAC was stimulated with 200 nM Gαs bound either to GDP or GTPγS at the indicated concentrations of FSK. (B) Complementation of SYNAC domains is enhanced by GTP-bound Gαs. FRET response of SYNAC stimulated with 200 nM Gαs bound either to GDP or GTPγS, with or without 1 μM FSK. (C) Complementation of SYNAC domains is synergistic to GTP-Gαs and FSK. FRET response of SYNAC with or without GTPγS bound Gαs (800 nM), in the presence of the indicated concentrations of FSK. Activity data are mean ± S.E.M. of three independent repeats using three different preparations of protein (both SYNAC and Gαs). FRET data are mean ± S.D. of three spectra. Significance assessed by Student’s t test (unpaired). n.s. = not statistically significant; *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001.