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The identification of novel cyclic AMP-dependent protein kinase anchoring proteins using bioinformatic filters and peptide arrays.

ABSTRACT: A-kinase anchoring proteins (AKAPs) localize cyclic AMP-dependent protein kinase (PKA) to specific regions in the cell and place PKA in proximity to its phosphorylation targets. A computational model was created to identify AKAPs that bind to the docking/dimerization domain of the RII alpha isoform of the regulatory subunit of PKA. The model was used to search the entire human proteome, and the top candidates were tested for an interaction using peptide array experiments. Verified interactions include sphingosine kinase interacting protein and retinoic acid-induced protein 16. These interactions highlight new signaling pathways mediated by PKA.

SUBMITTER: McLaughlin WA

PROVIDER: S-EPMC3038459 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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The identification of novel cyclic AMP-dependent protein kinase anchoring proteins using bioinformatic filters and peptide arrays.

McLaughlin William A WA Hou Tingjun T Taylor Susan S SS Wang Wei W

Protein engineering, design & selection : PEDS 20101129 3

A-kinase anchoring proteins (AKAPs) localize cyclic AMP-dependent protein kinase (PKA) to specific regions in the cell and place PKA in proximity to its phosphorylation targets. A computational model was created to identify AKAPs that bind to the docking/dimerization domain of the RII alpha isoform of the regulatory subunit of PKA. The model was used to search the entire human proteome, and the top candidates were tested for an interaction using peptide array experiments. Verified interactions i ...[more]

PMID: 21115539

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