Gene interactions and pathways from curated databases and text-mining

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PDE4D — PRKAR2A

Text-mined interactions from Literome

Beard et al., J Biol Chem 2000 : Mutation of the PKA substrate site in UCR1 ( Ser-54 ) to aspartic acid, which mimics the activation of PDE4D3 by PKA , profoundly reduced the interaction between UCR1 and UCR2
Dodge et al., EMBO J 2001 : Disruption of PKA- mAKAP interaction prevents this enhancement of PDE4D3 activity, suggesting that the proximity of both enzymes in the mAKAP signaling complex forms a negative feedback loop to restore basal cAMP levels
Ang et al., J Neurochem 2002 (Second Messenger Systems) : Together, these data show reciprocal regulation of PDE1C and PDE4D by PKA , which represents a novel scheme for plasticity in intracellular signalling
Carlisle Michel et al., Biochem J 2004 : In vitro and cellular experiments demonstrate that PKA-phosphorylation of PDE4D3 on Ser-13 increases the affinity of PDE4D3 for mAKAP
Dodge-Kafka et al., Nature 2005 (Hypertrophy) : Anchored PKA stimulates PDE4D3 to reduce local cAMP concentrations, whereas an mAKAP associated ERK5 kinase module suppresses PDE4D3
Millen et al., Eur J Cell Biol 2006 (Anoxia...) : Despite the hypoxia induced increases in the expression of PDE4A10/11, PDE4B2 and PDE4D5 and activation of certain of these long PDE4 isoforms through PKA phosphorylation, we suggest that the failure to see any overall increase in PDE4 activity is due to ERK mediated phosphorylation and inhibition of particular PDE4 long isoforms
Bolger et al., Biochem J 2006 : siRNA ( small interfering RNA ) -mediated knockdown of RACK1 in HEK-293 ( human embryonic kidney ) B2 cells increased beta-arrestin scaffolded PDE4D5 approx. 5-fold, increased PDE4D5 recruited to the beta2AR ( beta2-adrenergic receptor ) upon isoproterenol challenge approx. 4-fold and severely attenuated ( approx. 4-5 fold ) both isoproterenol stimulated PKA ( protein kinase A ) phosphorylation of the beta2AR and activation of ERK ( extracellular-signal regulated kinase )
Levallet et al., Biol Reprod 2007 : Resensitization of the cAMP response to FSH in 20-day-old Sertoli cells was also associated with the highest FSH induced transient increase in both soluble and particulate PDE4 activities, which suggests developmental changes in the PKA mediated upregulation of the catalytic activities of long PDE4D
Murthy et al., Am J Physiol Gastrointest Liver Physiol 2008 : We have previously shown that cAMP levels are regulated by PKA mediated phosphorylation of cAMP-specific phosphodiesterase 3A (PDE3A) and PDE4D5 ; the latter is the only PDE4D isoform expressed in smooth muscle
Bruss et al., J Biol Chem 2008 : This effect of PDE4D ablation was in large part due to inactivation of a negative feedback mechanism consisting of the PKA mediated activation of PDE4D in response to elevated cAMP levels, as indicated by experiments using the cAMP dependent protein kinase inhibitors H89 and PKI
Dodge-Kafka et al., J Biol Chem 2010 : Accordingly, expression of a B56delta mutant that can not be phosphorylated by PKA results in increased PDE4D3 phosphorylation
Oliveira et al., PloS one 2010 : Simulations further demonstrate that generation of the cAMP microdomain requires a pool of PDE4D anchored in the cytosol and also requires PKA mediated phosphorylation of PDE4D which increases its activity
Sakakibara et al., Neuroendocrinology 1998 : We hypothesize that activation of PDE4D3 by PKA may constitute a negative feedback signaling pathway which participates in the regulation of cAMP levels