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Literature summary for 3.1.4.53 extracted from

  • MacKenzie, K.F.; Wallace, D.A.; Hill, E.V.; Anthony, D.F.; Henderson, D.J.; Houslay, D.M.; Arthur, J.S.; Baillie, G.S.; Houslay, M.D.
    Phosphorylation of cAMP-specific PDE4A5 (phosphodiesterase-4A5) by MK2 (MAPKAPK2) attenuates its activation through protein kinase A phosphorylation (2011), Biochem. J., 435, 755-769.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus P54748
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of cAMP-specific PDE4A5 by MAPK-activated protein kinase 2, also called MAPKAPK2. PDE4A5 is phosphorylated at Ser147, within the regulatory UCR1, ultraconserved region 1, domain conserved among PDE4 long isoforms. Phosphorylation by MK2, although not altering PDE4A5 activity, markedly attenuates PDE4A5 activation through phosphorylation by protein kinase A. Phosphorylation by MK2 also triggers a conformational change in PDE4A5 that attenuates PDE4A5 interaction with proteins whose binding involves UCR2, such as DISC1 and AIP, but not the UCR2-independent interacting scaffold protein beta-arrestin Rattus norvegicus

Synonyms

Synonyms Comment Organism
cAMP-specific PDE4A5
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 Rattus norvegicus
PDE4
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 Rattus norvegicus
phosphodiesterase-4A5
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 Rattus norvegicus

General Information

General Information Comment Organism
physiological function cAMP-specific PDE 4 isoforms underpin compartmentalized cAMP signalling in mammalian cells through targeting to specific signalling complexes. Phosphorylation of PDE4A5 by MK2 confers the amplification of intracellular cAMP accumulation in response to adenylate cyclase activation by attenuating a major desensitization system to cAMP. Long PDE4 isoforms thus provide a novel node for cross-talk between the cAMP and p38 MAPK signalling systems at the level of MK2 Rattus norvegicus