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Interaction IDMol ATypeSpeciesVerbNatureMol BTypeSpecies
79168TNFProteinHomo sapiens-eIncreases activityindirectProtein kinase, cAMP-dependent, catalytic subunitSubunit groupHomo sapiens
Consistent with the hypothesis that TNF-alpha induces perilipin hyperphosphorylation by activating PKA, TNF-alpha increased intracellular cAMP approximately 1.7-fold, and the increase was abrogated by PD98059.
193130Protein kinase, cAMP-dependent, catalytic subunitSubunit groupHomo sapiens-eIncreases activityindirectTTF1ProteinHomo sapiens-e
We asked whether PKA directly activates TTF1. We show that cAMP/PKA activates pTg and a synthetic target promoter carrying TTF1 binding site repeats in several cell types. Activation depends on TTF1.Phosphopeptide mapping indicates that TTF1 is constitutively phosphorylated at multiple sites, and that cAMP stimulated phosphorylation of one site, serine 337, in vivo. However, alanine substitution at this residue or at all sites of phosphorylation did not reduce PKA activation of pTg. Thus, PKA stimulates TTF1 transcriptional activity in an indirect manner, perhaps by recruiting to or removing from the target promoter another regulatory factor(s).