Byrne, A. M., Elliott, C. , Hoffmann, R. and Baillie, G. S. (2015) The activity of cAMP-Phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus. FEBS Letters, 589(6), pp. 750-755. (doi: 10.1016/j.febslet.2015.02.004) (PMID:25680530) (PMCID:PMC4346272)
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Abstract
The cyclic AMP phosphodiesterases type 4 (PDE4s) are expressed in a cell specific manner, with intracellular targeting directed by unique N-terminal anchor domains. All long form PDE4s are phosphorylated and activated by PKA phosphorylation within their upstream conserved region 1 (UCR1). Here, we identify and characterise a novel PKA site (serine 42) within the N-terminal region of PDE4D7, an isoform whose activity is known to be important in prostate cancer progression and ischemic stroke. In contrast to the UCR1 site, PKA phosphorylation of the PDE4D7 N-terminus appears to occur constitutively and inhibits PDE4 activity to allow cAMP signalling under basal conditions.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Baillie, Professor George and Elliott, Dr Christina and Hoffmann, Dr Ralf |
| Authors: | Byrne, A. M., Elliott, C., Hoffmann, R., and Baillie, G. S. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Cardiovascular & Metabolic Health College of Medical Veterinary and Life Sciences > School of Life Sciences |
| Journal Name: | FEBS Letters |
| Publisher: | Elsevier B.V. |
| ISSN: | 0014-5793 |
| ISSN (Online): | 1873-3468 |
| Copyright Holders: | Copyright © 2015 The Authors |
| First Published: | First published in FEBS Letters 589(6):750-755 |
| Publisher Policy: | Reproduced under a Creative Commons License |
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