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@ARTICLE{Corradini:137502,
      author       = {Corradini, Eleonora and Vallur, Raghavan and Raaijmakers,
                      Linsey M and Feil, Susanne and Feil, Robert and Heck, Albert
                      J R and Scholten, Arjen},
      title        = {{A}lterations in the cerebellar ({P}hospho)proteome of a
                      cyclic guanosine monophosphate (c{GMP})-dependent protein
                      kinase knockout mouse.},
      journal      = {Molecular $\&$ cellular proteomics},
      volume       = {13},
      number       = {8},
      issn         = {1535-9476},
      address      = {Bethesda, Md.},
      publisher    = {The American Society for Biochemistry and Molecular
                      Biology},
      reportid     = {DZNE-2020-03824},
      pages        = {2004-2016},
      year         = {2014},
      abstract     = {The cyclic nucleotide cyclic guanosine monophosphate (cGMP)
                      plays an important role in learning and memory, but its
                      signaling mechanisms in the mammalian brain are not fully
                      understood. Using mass-spectrometry-based proteomics, we
                      evaluated how the cerebellum adapts its (phospho)proteome in
                      a knockout mouse model of cGMP-dependent protein kinase type
                      I (cGKI). Our data reveal that a small subset of proteins in
                      the cerebellum $(∼3\%$ of the quantified proteins) became
                      substantially differentially expressed in the absence of
                      cGKI. More changes were observed at the phosphoproteome
                      level, with hundreds of sites being differentially
                      phosphorylated between wild-type and knockout cerebellum.
                      Most of these phosphorylated sites do not represent known
                      cGKI substrates. An integrative computational network
                      analysis of the data indicated that the differentially
                      expressed proteins and proteins harboring differentially
                      phosphorylated sites largely belong to a tight network in
                      the Purkinje cells of the cerebellum involving important
                      cGMP/cAMP signaling nodes (e.g. PDE5 and PKARIIβ) and
                      Ca(2+) signaling (e.g. SERCA3). In this way, removal of cGKI
                      could be linked to impaired cerebellar long-term depression
                      at Purkinje cell synapses. In addition, we were able to
                      identify a set of novel putative (phospho)proteins to be
                      considered in this network. Overall, our data improve our
                      understanding of cerebellar cGKI signaling and suggest novel
                      players in cGKI-regulated synaptic plasticity.},
      keywords     = {Animals / Cerebellum: metabolism / Cyclic GMP / Cyclic
                      GMP-Dependent Protein Kinase Type I: genetics / Cyclic
                      GMP-Dependent Protein Kinase Type I: metabolism / Mice /
                      Mice, Knockout / Phosphoproteins: isolation $\&$
                      purification / Phosphorylation / Proteomics: methods /
                      Signal Transduction / Synapses: metabolism / Phosphoproteins
                      (NLM Chemicals) / Cyclic GMP-Dependent Protein Kinase Type I
                      (NLM Chemicals) / Prkg1 protein, mouse (NLM Chemicals) /
                      Cyclic GMP (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:24925903},
      pmc          = {pmc:PMC4125733},
      doi          = {10.1074/mcp.M113.035154},
      url          = {https://pub.dzne.de/record/137502},
}