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@ARTICLE{Kbler:127723,
      author       = {D. Kübler$^*$ and J. Seidler and S. André and S. Kumar
                      and R. Schwartz-Albiez$^*$ and W.-D. Lehmann$^*$ and H.-J.
                      Gabius},
      title        = {{P}hosphorylation of multifunctional galectins by protein
                      kinases {CK}1, {CK}2, and {PKA}.},
      journal      = {Analytical biochemistry},
      volume       = {449},
      issn         = {0003-2697},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2017-03746},
      pages        = {109 - 117},
      year         = {2014},
      abstract     = {Phosphorylation is known to have a strong impact on protein
                      functions. We analyzed members of the lectin family of
                      multifunctional galectins as targets of the protein kinases
                      CK1, CK2, and PKA. Galectins are potent growth regulators
                      able to bind both glycan and peptide motifs at intra- and
                      extracellular sites. Performing in vitro kinase assays,
                      galectin phosphorylation was detected by phosphoprotein
                      staining and autoradiography. The insertion of phosphoryl
                      groups varied to a large extent depending on the type of
                      kinase applied and the respective galectin substrate. Sites
                      of phosphorylation observed in the recombinant galectins
                      were determined by a strategic combination of phosphopeptide
                      enrichment and nano-ultra-performance liquid chromatography
                      tandem mass spectrometry (nanoUPLC-MS/MS). By in silico
                      modeling, phosphorylation sites were visualized
                      three-dimensionally. Our results reveal
                      galectin-type-specific Ser-/Thr-dependent phosphorylation
                      beyond the known example of galectin-3. These data are the
                      basis for functional studies and also illustrate the
                      analytical sensitivity of the applied methods for further
                      work on human lectins.},
      keywords     = {Galectins (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals) / Casein Kinase I (NLM Chemicals) / Casein Kinase
                      II (NLM Chemicals) / Cyclic AMP-Dependent Protein Kinases
                      (NLM Chemicals)},
      cin          = {A060 / D015 / W160},
      ddc          = {570},
      cid          = {I:(DE-He78)A060-20160331 / I:(DE-He78)D015-20160331 /
                      I:(DE-He78)W160-20160331},
      pnm          = {311 - Signalling pathways, cell and tumor biology
                      (POF3-311)},
      pid          = {G:(DE-HGF)POF3-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24333252},
      doi          = {10.1016/j.ab.2013.12.006},
      url          = {https://inrepo02.dkfz.de/record/127723},
}