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@ARTICLE{Hornbergs:972159,
      author       = {Hornbergs, Jannik and Montag, Karolin and Loschwitz,
                      Jennifer and Mohr, Inga and Poschmann, Gereon and Schnake,
                      Anika and Gratz, Regina and Brumbarova, Tzvetina and
                      Eutebach, Monique and Angrand, Kalina and Fink-Straube,
                      Claudia and Stühler, Kai and Zeier, Jürgen and Hartmann,
                      Laura and Strodel, Birgit and Ivanov, Rumen and Bauer,
                      Petra},
      title        = {{SEC}14-{GOLD} protein {PATELLIN}2 binds {IRON}-{REGULATED}
                      {TRANSPORTER}1 linking root iron uptake to vitamin {E}},
      journal      = {Plant physiology},
      volume       = {192},
      number       = {1},
      issn         = {0032-0889},
      address      = {Oxford},
      publisher    = {Oxford University Press},
      reportid     = {FZJ-2023-01103},
      pages        = {504–526},
      year         = {2022},
      abstract     = {Organisms require micronutrients, and Arabidopsis
                      (Arabidopsis thaliana) IRON-REGULATED TRANSPORTER1 (IRT1) is
                      essential for iron (Fe2+) acquisition into root cells.
                      Uptake of reactive Fe2+ exposes cells to the risk of
                      membrane lipid peroxidation. Surprisingly little is known
                      about how this is avoided. IRT1 activity is controlled by an
                      intracellular variable region (IRT1vr) that acts as a
                      regulatory protein interaction platform. Here, we describe
                      that IRT1vr interacted with peripheral plasma membrane
                      SEC14-Golgi dynamics (SEC14-GOLD) protein PATELLIN2 (PATL2).
                      SEC14 proteins bind lipophilic substrates and transport or
                      present them at the membrane. To date, no direct roles have
                      been attributed to SEC14 proteins in Fe import. PATL2
                      affected root Fe acquisition responses, interacted with ROS
                      response proteins in roots, and alleviated root lipid
                      peroxidation. PATL2 had high affinity in vitro for the major
                      lipophilic antioxidant vitamin E compound α-tocopherol.
                      Molecular dynamics simulations provided insight into
                      energetic constraints and the orientation and stability of
                      the PATL2-ligand interaction in atomic detail. Hence, this
                      work highlights a compelling mechanism connecting vitamin E
                      with root metal ion transport at the plasma membrane with
                      the participation of an IRT1-interacting and
                      α-tocopherol-binding SEC14 protein.},
      cin          = {IBI-7},
      ddc          = {580},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36493393},
      UT           = {WOS:000927167100001},
      doi          = {10.1093/plphys/kiac563},
      url          = {https://juser.fz-juelich.de/record/972159},
}