The activity of cAMP-phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus

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 i...

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Autores principales: Byrne, Ashleigh M., Elliott, Christina, Hoffmann, Ralf, Baillie, George S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Science B.V 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4346272/
https://www.ncbi.nlm.nih.gov/pubmed/25680530
http://dx.doi.org/10.1016/j.febslet.2015.02.004
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author Byrne, Ashleigh M.
Elliott, Christina
Hoffmann, Ralf
Baillie, George S.
author_facet Byrne, Ashleigh M.
Elliott, Christina
Hoffmann, Ralf
Baillie, George S.
author_sort Byrne, Ashleigh M.
collection PubMed
description 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.
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spelling pubmed-43462722015-03-12 The activity of cAMP-phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus Byrne, Ashleigh M. Elliott, Christina Hoffmann, Ralf Baillie, George S. FEBS Lett Article 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. Elsevier Science B.V 2015-03-12 /pmc/articles/PMC4346272/ /pubmed/25680530 http://dx.doi.org/10.1016/j.febslet.2015.02.004 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Byrne, Ashleigh M.
Elliott, Christina
Hoffmann, Ralf
Baillie, George S.
The activity of cAMP-phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus
title The activity of cAMP-phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus
title_full The activity of cAMP-phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus
title_fullStr The activity of cAMP-phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus
title_full_unstemmed The activity of cAMP-phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus
title_short The activity of cAMP-phosphodiesterase 4D7 (PDE4D7) is regulated by protein kinase A-dependent phosphorylation within its unique N-terminus
title_sort activity of camp-phosphodiesterase 4d7 (pde4d7) is regulated by protein kinase a-dependent phosphorylation within its unique n-terminus
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4346272/
https://www.ncbi.nlm.nih.gov/pubmed/25680530
http://dx.doi.org/10.1016/j.febslet.2015.02.004
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