July 1, 1996Journal of Biological ChemistryOpen Access

Phosphorylation and Activation of a cAMP-specific Phosphodiesterase by the cAMP-dependent Protein Kinase

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Population

Recombinant rat PDE4D3 and MA-10 cells expressing wild type and mutated PDE4D3 proteins

Comparison

PKA-dependent phosphorylation and site-directed… vs Wild-type PDE4D3 or unphosphorylated state

Design

Preclinical

Authors

CSClaudio SetteUniversità Cattolica del Sacro Cuore MCMarco ContiUniversité Paris-Sud

Discussion

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Implication

Ser54 may be a regulatory target in PDE4D3; leaves open its role in cardiac cAMP signaling pending in vivo validation.

Structured PICO

Population

Recombinant rat PDE4D3 and MA-10 cells expressing wild type and mutated PDE4D3 proteins

Intervention

PKA-dependent phosphorylation (via ATP and PKA catalytic subunit in vitro, or dibutyryl cAMP in intact cells) and site-directed mutagenesis (Ser13 to Ala, Ser54 to Ala)

Comparator

Wild-type PDE4D3 or unphosphorylated state

Outcome

PDE4D3 enzyme activation and phosphorylation statussurrogate

The Ser54 residue in the amino terminus regulatory domain of PDE4D3 is essential for its activation by PKA-dependent phosphorylation.

Cite This Study

Sette et al. (1996) studied this question.

synapsesocial.com/papers/6a709dce87f921057127cab1 https://doi.org/10.1074/jbc.271.28.16526

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Phosphorylation and Activation of a cAMP-specific Phosphodiesterase by the cAMP-dependent Protein Kinase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Phosphorylation and Activation of a cAMP-specific Phosphodiesterase by the cAMP-dependent Protein Kinase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider