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The Activity of cAMP-phosphodiesterase 4D7 (PDE4D7) Is Regulated by Protein Kinase A-dependent Phosphorylation Within Its Unique N-terminus

The Activity of cAMP-phosphodiesterase 4D7 (PDE4D7) Is Regulated by Protein Kinase A-dependent Phosphorylation Within Its Unique N-terminus

Ashleigh M Byrne, Christina Elliott, Ralf Hoffmann, George S Baillie

FEBS Lett. 2015 Mar 12;589(6):750-5.

PMID: 25680530

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4245719	PDE4D7 active human			Price

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