Related Experiment Video
Updated: May 21, 2026

Mapping the Cellular Distribution of an Optogenetic Protein Using a Light-Stimulation Grid
Published on: January 26, 2024
Cyclic AMP-specific phosphodiesterase, PDE8A1, is activated by protein kinase A-mediated phosphorylation
Kim M Brown1, Louisa C Y Lee, Jane E Findlay
1Institute of Cardiovascular and Medical Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.
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.
More Related Videos
Related Concept Videos
cAMP-dependent Protein Kinase Pathways
GPCRs Regulate Adenylyl Cylase Activity
Two...
Amplifying Signals via Enzymatic Cascade
Intracellular Signaling Cascades
Amplifying Signals via Second Messengers
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

