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Literature summary for 3.1.4.53 extracted from

  • Dodge-Kafka, K.L.; Bauman, A.; Mayer, N.; Henson, E.; Heredia, L.; Ahn, J.; McAvoy, T.; Nairn, A.C.; Kapiloff, M.S.
    cAMP-stimulated protein phosphatase 2A activity associated with muscle A kinase-anchoring protein (mAKAP) signaling complexes inhibits the phosphorylation and activity of the cAMP-specific phosphodiesterase PDE4D3 (2010), J. Biol. Chem., 285, 11078-11086.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in HEK-293 cells Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3',5'-cAMP + H2O Rattus norvegicus
-
5'-AMP
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein protein kinase A catalyzes phosphorylation (at Ser-54) and activation of isoform PDE4D3. Protein phosphatase 2A associated with muscle A kinase-anchoring protein complexes promotes PDE4D3 dephosphorylation at Ser-54 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
cardiomyocyte
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3',5'-cAMP + H2O
-
Rattus norvegicus 5'-AMP
-
?

Synonyms

Synonyms Comment Organism
cAMP-specific phosphodiesterase
-
Rattus norvegicus
PDE4D3 isoform Rattus norvegicus

Expression

Organism Comment Expression
Rattus norvegicus forskolin treatment alone is unable to stimulate mAKAP-bound PDE4D3 activity significantly in HEK-293 cells, whereas forskolin (0.05 mM) and okadaic acid (0.3 mM) treatment together synergistically increase PDE4D3 activity up