PP2A dephosphorylates serine-715 of PDE4D5 in p-S715-PDE4D5:integrin alpha5:integrin beta1:fibronectin

Stable Identifier
R-HSA-9865238
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Interaction between integrin alpha5 (ITGA5) and fibronectin causes ITGA5 to recruit p-S715-PDE4D5, which then binds the PPP2R2A (B55alpha) subunit of the protein phosphatase PP2A (PPP2CA:PPP2R2A:PPP2R1A,B) (inferred from bovine homologs). The PPP2CA subunit of PP2A subsequently binds PPP2R2A and dephosphorylates serine-715 of PDE4D5 (inferred from bovine homologs). Dephosphorylation of PDE4D5 is thought to increase its phosphodiesterase activity, which causes hydrolysis of cAMP. Cyclic AMP is anti-inflammatory due to its enhancement of PKA activity (Funk et al. 2010), therefore PDE4D5 appears to be pro-inflammatory.
Participants
Participates
Catalyst Activity

protein serine/threonine phosphatase activity of p-S26-ANXA2:PP2A:p-S715-PDE4D5:ITGA5:ITGB1:fibronectin [plasma membrane]

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