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Phosphorylation of PDE4A5 by MAPKAPK2 attenuates fibrin degradation via p75 signalling.

ABSTRACT: Phosphodiesterases (PDEs) shape local cAMP gradients to underpin the specificity of receptor function. Key to this process is the highly defined nature of the intra-cellular location of PDEs in the cell. PDE4A5 is a PDE isoform that specifically degrades cAMP and is known to associate with the p75 neurotrophin receptor (p75NTR) where it modulates cAMP signalling cascades that regulate extracellular matrix remodelling in the lungs. Here we map and validate novel protein-protein interaction sites that are important for formation of the PDE4A5-p75NTR complex and show, for the first time, that phosphorylation of PDE4A5 by MAPKAPK2 enhances PDE4A5 interaction with p75NTR and that this, in turn, serves to attenuate fibrin degradation.

SUBMITTER: Houslay KF 

PROVIDER: S-EPMC6607969 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

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Phosphorylation of PDE4A5 by MAPKAPK2 attenuates fibrin degradation via p75 signalling.

Houslay K F KF   Fertig B A BA   Christian F F   Tibbo A J AJ   Ling J J   Findlay J E JE   Houslay M D MD   Baillie G S GS  

Journal of biochemistry 20190701 1

Phosphodiesterases (PDEs) shape local cAMP gradients to underpin the specificity of receptor function. Key to this process is the highly defined nature of the intra-cellular location of PDEs in the cell. PDE4A5 is a PDE isoform that specifically degrades cAMP and is known to associate with the p75 neurotrophin receptor (p75NTR) where it modulates cAMP signalling cascades that regulate extracellular matrix remodelling in the lungs. Here we map and validate novel protein-protein interaction sites  ...[more]