biostudies-literatureMcLaughlin WANIDDK NIH HHS333-9https://www.ebi.ac.uk/biostudies/studies/S-EPMC3038459biostudies-literatureUnknown24(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 include sphingosine kinase interacting protein and retinoic acid-induced protein 16. These interactions highlight new signaling pathways mediated by PKA.Protein engineering, design & selection : PEDSThe identification of novel cyclic AMP-dependent protein kinase anchoring proteins using bioinformatic filters and peptide arrays.PMC3038459T32DK07233P01 DK054441P01 DK54441McLaughlin WAHou TTaylor SSWang WfalseThe identification of novel cyclic AMP-dependent protein kinase anchoring proteins using bioinformatic filters and peptide arrays.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.2011-01-01T00:00:00Z2011 Mar2020-11-19T15:29:16Z2019-03-27T00:38:54ZS-EPMC30384592111553910.1093/protein/gzq106