PKA-phosphorylation of PDE4D3 facilitates recruitment of the mAKAP signalling complex

Biochem J. 2004 Aug 1;381(Pt 3):587-92. doi: 10.1042/BJ20040846.

Abstract

mAKAP (muscle-selective A-kinase-anchoring protein) co-ordinates a cAMP-sensitive negative-feedback loop comprising PKA (cAMP-dependent protein kinase) and the cAMP-selective PDE4D3 (phosphodiesterase 4D3). In vitro and cellular experiments demonstrate that PKA-phosphorylation of PDE4D3 on Ser-13 increases the affinity of PDE4D3 for mAKAP. Our data suggest that activation of mAKAP-anchored PKA enhances the recruitment of PDE4D3, allowing for quicker signal termination.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3',5'-Cyclic-AMP Phosphodiesterases / metabolism*
  • Adaptor Proteins, Signal Transducing / physiology*
  • Binding Sites
  • Cyclic AMP-Dependent Protein Kinases / metabolism*
  • Cyclic Nucleotide Phosphodiesterases, Type 4
  • Enzyme Activation / physiology
  • Humans
  • Kidney / cytology
  • Kidney / embryology
  • Kidney / enzymology
  • Molecular Mimicry / physiology
  • Peptide Fragments / metabolism
  • Peptides / metabolism
  • Phosphorylation
  • Protein Binding / physiology
  • Protein Interaction Mapping
  • Serine / metabolism

Substances

  • Adaptor Proteins, Signal Transducing
  • Peptide Fragments
  • Peptides
  • Serine
  • Cyclic AMP-Dependent Protein Kinases
  • 3',5'-Cyclic-AMP Phosphodiesterases
  • Cyclic Nucleotide Phosphodiesterases, Type 4