PDE7A1, a cAMP-specific phosphodiesterase, inhibits cAMP-dependent protein kinase by a direct interaction with C.
作者： Ping Han , Pushpalatha Sonati , Charles Rubin , Tamar Michaeli
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摘要: Abstract The N-terminal regulatory region of the high affinity cAMP-specific phosphodiesterase, PDE7A1, contains two copies cAMP-dependent kinase (PKA) pseudosubstrate site RRGAI. In βTC3 insulinoma cells, PDE7A1 co-localizes with PKA II in Golgi-centrosome region. roles and its play cAMP signaling were examined by studying interactions subunits. associates dissociated C subunit (C), but does not bind tetrameric holoenzyme. High binding inhibits activity vitro (IC50 = 0.5 nm). domain containing sites at N terminus mediates complex formation C. repeat CHO-K1 cells also suppresses dependent, cAMP-independent, physiological responses yeast. Thus, possesses a non-catalytic that can contribute to termination signals via direct inhibition This study identifies novel inhibitor affect cyclic nucleotide phosphodiesterase.
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