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Cyclic AMP‐specific phosphodiesterase, PDE8A1, is activated by protein kinase A‐mediated phosphorylation
Author(s) -
Brown Kim M.,
Lee Louisa C.Y.,
Findlay Jane E.,
Day Jonathan P.,
Baillie George S.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.04.033
Subject(s) - phosphodiesterase , phosphorylation , protein kinase a , microbiology and biotechnology , pde10a , serine , chemistry , enzyme , chemotaxis , enzyme activator , kinase , biochemistry , biology , receptor
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.