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@ARTICLE{Lievens:138728,
      author       = {Lievens, Patricia Marie-Jeanne and Kuznetsova, Tatiana and
                      Kochlamazashvili, Gaga and Cesca, Fabrizia and Gorinski,
                      Natalya and Galil, Dalia Abdel and Cherkas, Volodimir and
                      Ronkina, Natalia and Lafera, Juri and Gaestel, Matthias and
                      Ponimaskin, Evgeni and Dityatev, Alexander},
      title        = {{ZDHHC}3 {T}yrosine {P}hosphorylation {R}egulates {N}eural
                      {C}ell {A}dhesion {M}olecule {P}almitoylation.},
      journal      = {Molecular and cellular biology},
      volume       = {36},
      number       = {17},
      issn         = {0270-7306},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {DZNE-2020-05050},
      pages        = {2208-2225},
      year         = {2016},
      abstract     = {The neural cell adhesion molecule (NCAM) mediates cell-cell
                      and cell-matrix adhesion. It is broadly expressed in the
                      nervous system and regulates neurite outgrowth,
                      synaptogenesis, and synaptic plasticity. Previous in vitro
                      studies revealed that palmitoylation of NCAM is required for
                      fibroblast growth factor 2 (FGF2)-stimulated neurite
                      outgrowth and identified the zinc finger DHHC
                      (Asp-His-His-Cys)-containing proteins ZDHHC3 and ZDHHC7 as
                      specific NCAM-palmitoylating enzymes. Here, we verified that
                      FGF2 controlled NCAM palmitoylation in vivo and investigated
                      molecular mechanisms regulating NCAM palmitoylation by
                      ZDHHC3. Experiments with overexpression and pharmacological
                      inhibition of FGF receptor (FGFR) and Src revealed that
                      these kinases control tyrosine phosphorylation of ZDHHC3 and
                      that ZDHHC3 is phosphorylated by endogenously expressed FGFR
                      and Src proteins. By site-directed mutagenesis, we found
                      that Tyr18 is an FGFR1-specific ZDHHC3 phosphorylation site,
                      while Tyr295 and Tyr297 are specifically phosphorylated by
                      Src kinase in cell-based and cell-free assays. Abrogation of
                      tyrosine phosphorylation increased ZDHHC3
                      autopalmitoylation, enhanced interaction with NCAM, and
                      upregulated NCAM palmitoylation. Expression of ZDHHC3 with
                      tyrosine mutated in cultured hippocampal neurons promoted
                      neurite outgrowth. Our findings for the first time highlight
                      that FGFR- and Src-mediated tyrosine phosphorylation of
                      ZDHHC3 modulates ZDHHC3 enzymatic activity and plays a role
                      in neuronal morphogenesis.},
      keywords     = {Acyltransferases: genetics / Acyltransferases: metabolism /
                      Animals / Cells, Cultured / Fibroblast Growth Factor 2:
                      metabolism / Gene Expression Regulation / Lipoylation /
                      Membrane Proteins: genetics / Membrane Proteins: metabolism
                      / Mice / Mutation / Neural Cell Adhesion Molecules:
                      metabolism / Neurites: metabolism / Phosphorylation /
                      Receptors, Fibroblast Growth Factor: metabolism / Tyrosine:
                      genetics / Tyrosine: metabolism / src-Family Kinases:
                      metabolism / GODZ protein, mouse (NLM Chemicals) / Membrane
                      Proteins (NLM Chemicals) / Neural Cell Adhesion Molecules
                      (NLM Chemicals) / Receptors, Fibroblast Growth Factor (NLM
                      Chemicals) / Fibroblast Growth Factor 2 (NLM Chemicals) /
                      Tyrosine (NLM Chemicals) / Acyltransferases (NLM Chemicals)
                      / src-Family Kinases (NLM Chemicals)},
      cin          = {AG Dityatev},
      ddc          = {570},
      cid          = {I:(DE-2719)1310007},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27247265},
      pmc          = {pmc:PMC4985929},
      doi          = {10.1128/MCB.00144-16},
      url          = {https://pub.dzne.de/record/138728},
}