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
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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3',5'-Cyclic-AMP Phosphodiesterases / metabolism*
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Adaptor Proteins, Signal Transducing / physiology*
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Binding Sites
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Cyclic AMP-Dependent Protein Kinases / metabolism*
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Cyclic Nucleotide Phosphodiesterases, Type 4
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Enzyme Activation / physiology
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Humans
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Kidney / cytology
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Kidney / embryology
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Kidney / enzymology
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Molecular Mimicry / physiology
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Peptide Fragments / metabolism
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Peptides / metabolism
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Phosphorylation
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Protein Binding / physiology
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Protein Interaction Mapping
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Serine / metabolism
Substances
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Adaptor Proteins, Signal Transducing
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Peptide Fragments
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Peptides
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Serine
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Cyclic AMP-Dependent Protein Kinases
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3',5'-Cyclic-AMP Phosphodiesterases
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Cyclic Nucleotide Phosphodiesterases, Type 4