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Because domain A is fairly inaccessible to cAMP binding until cAMP binds to domain B, domain B provides been specified the “gatekeeper” for protein kinase A activation. The R368X mutation we identified causes a truncation of PRKAR1A domain B, like the deletion of two residues, R368 and tyrosine at position 373 , that have been shown to be determinant for the binding of cAMP to domain B.12 The substitution of the tyrosine 373 by alanine has been shown in vitro to render protein kinase A less sensitive to cAMP activation.12 These observations indicate that R368X should result in a functional defect in PRKAR1A that’s like the defect due to Y373A, with the resultant formation of protein kinase A tetramers whose activation by cAMP is impaired. Showing this at a molecular level, we compared cAMP-stimulated protein kinase A activity in cells transfected with vectors expressing the mutant complementary DNA that gives rise to the PRKAR1A amino acid mutations R368X and Y373A, cDNA corresponding to wild-type PRKAR1A, and an empty control vector.15,16 Wild-type and abnormal PRKAR1A proteins were expressed at similar amounts in these cells, which were greater than the endogenous PRKAR1A protein levels Activity in Cells Expressing R368X and Y373A PRKAR1A.).