Cyclic AMP-specific phosphodiesterase, PDE8A1, is activated by protein kinase A-mediated phosphorylation.

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Citation

Brown KM, Lee LC, Findlay JE, Day JP, Baillie GS

Cyclic AMP-specific phosphodiesterase, PDE8A1, is activated by protein kinase A-mediated phosphorylation.

FEBS Lett. 2012 Jun 4;586(11):1631-7. doi: 10.1016/j.febslet.2012.04.033. Epub 2012 May 3.

PubMed ID
22673573 [ View in PubMed
]
Abstract

The cyclic AMP-specific phosphodiesterase PDE8 has been shown to play a pivotal role in important processes such as steroidogenesis, T cell adhesion, regulation of heart beat and chemotaxis. However, no information exists on how the activity of this enzyme is regulated. We show that under elevated cAMP conditions, PKA acts to phosphorylate PDE8A on serine 359 and this action serves to enhance the activity of the enzyme. This is the first indication that PDE8 activity can be modulated by a kinase, and we propose that this mechanism forms a feedback loop that results in the restoration of basal cAMP levels.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8AO60658Details