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

Autor: Houslay KF; Department of Respiratory, Inflammation and Autoimmunity, MedImmune, Granta Park, Cambridge, UK., Fertig BA; Institute of Cardiovascular and Medical Sciences, University of Glasgow, Glasgow, UK., Christian F; Institute of Cardiovascular and Medical Sciences, University of Glasgow, Glasgow, UK., Tibbo AJ; Institute of Cardiovascular and Medical Sciences, University of Glasgow, Glasgow, UK., Ling J; Institute of Cardiovascular and Medical Sciences, University of Glasgow, Glasgow, UK., Findlay JE; Institute of Cancer Studies and Pharmaceutical Science, King's College, 150 Stamford Street, London, UK., Houslay MD; Institute of Cancer Studies and Pharmaceutical Science, King's College, 150 Stamford Street, London, UK., Baillie GS; Institute of Cardiovascular and Medical Sciences, University of Glasgow, Glasgow, UK.
Jazyk: angličtina
Zdroj: Journal of biochemistry [J Biochem] 2019 Jul 01; Vol. 166 (1), pp. 97-106.
DOI: 10.1093/jb/mvz016
Abstrakt: 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.
(© The Author(s) 2019. Published by Oxford University Press on behalf of the Japanese Biochemical Society.)
Databáze: MEDLINE
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