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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Byrne AM,Elliott C,Hoffmann R,Baillie GS

doi

10.1016/j.febslet.2015.02.004

subject

Has Abstract

pub_date

2015-03-12 00:00:00

pages

750-5

issue

6

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(15)00073-3

journal_volume

589

pub_type

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