The 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.
Department of Basic Science, The Commonwealth Medical College, 501 Madison Avenue, Scranton, PA 18510, USA. wmclaughlin@tcmedc.org
William A
WA
McLaughlin
Tingjun
T
Hou
Susan S
SS
Taylor
Wei
W
Wang
D054758:A Kinase Anchor Proteins / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D019295:Computational Biology / Q000379:methods*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D040081:Protein Array Analysis / Q000379:methods*; D015203:Reproducibility of Results; D015398:Signal Transduction
D054758:A Kinase Anchor Proteins; D017868:Cyclic AMP-Dependent Protein Kinases