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      Delineation of type I protein kinase A-selective signaling events using an RI anchoring disruptor.

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          Abstract

          Control of specificity in cAMP signaling is achieved by A-kinase anchoring proteins (AKAPs), which assemble cAMP effectors such as protein kinase A (PKA) into multiprotein signaling complexes in the cell. AKAPs tether the PKA holoenzymes at subcellular locations to favor the phosphorylation of selected substrates. PKA anchoring is mediated by an amphipathic helix of 14-18 residues on each AKAP that binds to the R subunit dimer of the PKA holoenzymes. Using a combination of bioinformatics and peptide array screening, we have developed a high affinity-binding peptide called RIAD (RI anchoring disruptor) with >1000-fold selectivity for type I PKA over type II PKA. Cell-soluble RIAD selectively uncouples cAMP-mediated inhibition of T cell function and inhibits progesterone synthesis at the mitochondria in steroid-producing cells. This study suggests that these processes are controlled by the type I PKA holoenzyme and that RIAD can be used as a tool to define anchored type I PKA signaling events.

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          Author and article information

          Journal
          J Biol Chem
          The Journal of biological chemistry
          American Society for Biochemistry & Molecular Biology (ASBMB)
          0021-9258
          0021-9258
          Jul 28 2006
          : 281
          : 30
          Affiliations
          [1 ] Biotechnology Centre of Oslo, University of Oslo, PB 1125 Blindern, N-0317, Oslo, Norway; Howard Hughes Medical Institute, Vollum Institute, Oregon Health and Science University, Portland, Oregon 97239. Electronic address: cathrine.carlson@biotek.uio.no.
          [2 ] Biotechnology Centre of Oslo, University of Oslo, PB 1125 Blindern, N-0317, Oslo, Norway; Howard Hughes Medical Institute, Vollum Institute, Oregon Health and Science University, Portland, Oregon 97239.
          [3 ] Biotechnology Centre of Oslo, University of Oslo, PB 1125 Blindern, N-0317, Oslo, Norway.
          [4 ] Howard Hughes Medical Institute, Vollum Institute, Oregon Health and Science University, Portland, Oregon 97239.
          Article
          S0021-9258(18)95280-4
          10.1074/jbc.M603223200
          16728392
          b20173e8-4f9c-44cf-8407-18b71710d481
          History

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