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@ARTICLE{Vallur:137446,
      author       = {Vallur, Raghavan and Kalbacher, Hubert and Feil, Robert},
      title        = {{C}atalytic activity of c{GMP}-dependent protein kinase
                      type {I} in intact cells is independent of {N}-terminal
                      autophosphorylation.},
      journal      = {PLOS ONE},
      volume       = {9},
      number       = {6},
      issn         = {1932-6203},
      address      = {San Francisco, California, US},
      publisher    = {PLOS},
      reportid     = {DZNE-2020-03768},
      pages        = {e98946},
      year         = {2014},
      abstract     = {Although cGMP-dependent protein kinase type I (cGKI) is an
                      important mediator of cGMP signaling and upcoming drug
                      target, its in vivo-biochemistry is not well understood.
                      Many studies showed that purified cGKI autophosphorylates
                      multiple sites at its N-terminus. Autophosphorylation might
                      be involved in kinase activation, but it is unclear whether
                      this happens also in intact cells. To study cGKI
                      autophosphorylation in vitro and in vivo, we have generated
                      phospho-specific antisera against major in
                      vitro-autophosphorylation sites of the cGKI isoforms, cGKIα
                      and cGKIβ. These antisera detected specifically and with
                      high sensitivity phospho-cGKIα (Thr58), phospho-cGKIα
                      (Thr84), or phospho-cGKIβ (Thr56/Ser63/Ser79). Using these
                      antisera, we show that ATP-induced autophosphorylation of
                      cGKI in purified preparations and cell extracts did neither
                      require nor induce an enzyme conformation capable of
                      substrate heterophosphorylation; it was even inhibited by
                      pre-incubation with cGMP. Interestingly, phospho-cGKI
                      species were not detectable in intact murine cells and
                      tissues, both under basal conditions and after induction of
                      cGKI catalytic activity. We conclude that N-terminal
                      phosphorylation, although readily induced in vitro, is not
                      required for the catalytic activity of cGKIα and cGKIβ in
                      vivo. These results will also inform screening strategies to
                      identify novel cGKI modulators.},
      keywords     = {Animals / Catalysis / Cattle / Cyclic GMP-Dependent Protein
                      Kinase Type I: chemistry / Cyclic GMP-Dependent Protein
                      Kinase Type I: immunology / Cyclic GMP-Dependent Protein
                      Kinase Type I: metabolism / Immune Sera: immunology / Mice /
                      Phosphorylation / Protein Interaction Domains and Motifs /
                      Protein Isoforms / Recombinant Proteins: chemistry /
                      Recombinant Proteins: metabolism / Substrate Specificity /
                      Immune Sera (NLM Chemicals) / Protein Isoforms (NLM
                      Chemicals) / Recombinant Proteins (NLM Chemicals) / Cyclic
                      GMP-Dependent Protein Kinase Type I (NLM Chemicals)},
      cin          = {AG N.N. 3},
      ddc          = {610},
      cid          = {I:(DE-2719)1240015},
      pnm          = {344 - Clinical and Health Care Research (POF3-344)},
      pid          = {G:(DE-HGF)POF3-344},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24897423},
      pmc          = {pmc:PMC4045857},
      doi          = {10.1371/journal.pone.0098946},
      url          = {https://pub.dzne.de/record/137446},
}