Dynamics of phosphodiesterase-induced cAMP dissociation from protein kinase A: capturing transient ternary complexes by HDXMS.

@article{Krishnamurthy2013DynamicsOP,
  title={Dynamics of phosphodiesterase-induced cAMP dissociation from protein kinase A: capturing transient ternary complexes by HDXMS.},
  author={Srinath Krishnamurthy and Balakrishnan Shenbaga Moorthy and Lin Liqin and Ganesh S. Anand},
  journal={Biochimica et biophysica acta},
  year={2013},
  volume={1834 6},
  pages={1215-21}
}
cAMP signaling is a fundamental cellular process necessary for mediating responses to hormonal stimuli. In contrast to cAMP-dependent activation of protein kinase A (PKA), an important cellular target, far less is known on termination in cAMP signaling, specifically how phosphodiesterases (PDEs) facilitate dissociation and hydrolysis of bound cAMP. In this study, we have probed the dynamics of a ternary complex of PKA and a PDE-RegA with an excess of a PDE-nonhydrolyzable cAMP analog, Sp-cAMPS… CONTINUE READING