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PPP2CA — PRKAR1B

Text-mined interactions from Literome

Ahn et al., Proc Natl Acad Sci U S A 2007 : The B56delta subunit is phosphorylated by PKA , and this increases the overall activity of PP2A in vitro and in vivo
Hsiung et al., J Neurosci Res 2008 : Our data suggest a central role of cAMP/PKA dependent PP2A in shifting the homeostasis of intracellular signaling downstream of activated 5-HT(1A) receptor toward cell death in biological systems linked to neuropsychiatric disorders
Hong et al., J Biol Chem 2008 : Here we show that ( i ) upstream regulators, PIK and PDK1, are not the target ( s ) of the cAMP inhibitory action ; ( ii ) constitutively active Akt and calyculin A-stimulated Akt are resistant to cAMP inhibition, suggesting the action of a phosphatase ; ( iii ) cAMP increases the rate of Akt dephosphorylation, directly implicating an Akt-phosphatase ; ( iv ) Epac- and protein kinase A (PKA)-specific analogs synergistically inhibit Akt, indicating the involvement of both cAMP dependent effector pathways ; ( v ) H89 and dominant negative Epac 279E block cAMP-inhibitory action ; ( vi ) Epac associates in a complex with Akt and PP2A, and the associated-phosphatase activity is positively modulated by cAMP in a PKA- and Rap1 dependent manner ; ( vii ) like its action on Akt inhibition, PKA- and Epac-specific analogs synergistically activate Epac associated PP2A ; and ( viii ) dominant negative PP2A blocks cAMP-inhibitory action