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@ARTICLE{Jansen:626508,
      author       = {Jansen, Séverine and Narasimhan, Subhash and Cabre
                      Fernandez, Paula and Iľkovičová, Lucia and Kozeleková,
                      Aneta and Králová, Kateřina and Hritz, Jozef and Žídek,
                      Lukáš},
      title        = {{C}haracterization of multiple binding sites on microtubule
                      associated protein 2c recognized by dimeric and monomeric
                      14‐3‐3ζ},
      journal      = {The FEBS journal},
      volume       = {292},
      number       = {8},
      issn         = {0014-2956},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {PUBDB-2025-01461},
      pages        = {1991 - 2016},
      year         = {2025},
      abstract     = {Microtubule associated protein 2 (MAP2) interacts with the
                      regulatory protein 14-3-3ζ in a cAMP-dependent protein
                      kinase (PKA) phosphorylation dependent manner. Using
                      selective phosphorylation, calorimetry, nuclear magnetic
                      resonance, chemical crosslinking, and X-ray crystallography,
                      we characterized interactions of 14-3-3ζ with various
                      binding regions of MAP2c. Although PKA phosphorylation
                      increases the affinity of MAP2c for 14-3-3ζ in the proline
                      rich region and C-terminal domain, unphosphorylated MAP2c
                      also binds the dimeric 14-3-3ζ via its microtubule binding
                      domain and variable central domain. Monomerization of
                      14-3-3ζ leads to the loss of affinity for the
                      unphosphorylated residues. In neuroblastoma cell extract,
                      MAP2c is heavily phosphorylated by PKA and the proline
                      kinase ERK2. Although 14-3-3ζ dimer or monomer do not
                      interact with the residues phosphorylated by ERK2, ERK2
                      phosphorylation of MAP2c in the C-terminal domain reduces
                      the binding of MAP2c to both oligomeric variants of
                      14-3-3ζ.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39877981},
      UT           = {WOS:001408033600001},
      doi          = {10.1111/febs.17405},
      url          = {https://bib-pubdb1.desy.de/record/626508},
}