@article{PoxsonKaradyGabrielssonetal.2017,
  author    = {Poxson, David J. and Karady, Michal and Gabrielsson, Roger and Alkattan, Aziz Y. and Gustavsson, Anna and Doyle, Siamsa M. and Robert, Stephanie and Ljung, Karin and Grebe, Markus and Simon, Daniel T. and Berggren, Magnus},
  title     = {Regulating plant physiology with organic electronics},
  series = {Proceedings of the National Academy of Sciences of the United States of America},
  volume    = {114},
  journal   = {Proceedings of the National Academy of Sciences of the United States of America},
  publisher = {National Acad. of Sciences},
  address   = {Washington},
  issn      = {0027-8424},
  doi       = {10.1073/pnas.1617758114},
  pages     = {4597 -- 4602},
  year      = {2017},
  abstract  = {The organic electronic ion pump (OEIP) provides flow-free and accurate delivery of small signaling compounds at high spatio-temporal resolution. To date, the application of OEIPs has been limited to delivery of nonaromatic molecules to mammalian systems, particularly for neuroscience applications. However, many long-standing questions in plant biology remain unanswered due to a lack of technology that precisely delivers plant hormones, based on cyclic alkanes or aromatic structures, to regulate plant physiology. Here, we report the employment of OEIPs for the delivery of the plant hormone auxin to induce differential concentration gradients and modulate plant physiology. We fabricated OEIP devices based on a synthesized dendritic polyelectrolyte that enables electrophoretic transport of aromatic substances. Delivery of auxin to transgenic Arabidopsis thaliana seedlings in vivo was monitored in real time via dynamic fluorescent auxin-response reporters and induced physiological responses in roots. Our results provide a starting point for technologies enabling direct, rapid, and dynamic electronic interaction with the biochemical regulation systems of plants.},
  language  = {en}
}
@article{MajdaGronesSintornetal.2017,
  author    = {Majda, Mateusz and Grones, Peter and Sintorn, Ida-Maria and Vain, Thomas and Milani, Pascale and Krupinski, Pawel and Zagorska-Marek, Beata and Viotti, Corrado and Jonsson, Henrik and Mellerowicz, Ewa J. and Hamant, Olivier and Robert, Stephanie},
  title     = {Mechanochemical Polarization of Contiguous Cell Walls Shapes Plant Pavement Cells},
  series = {Developmental cell},
  volume    = {43},
  journal   = {Developmental cell},
  publisher = {Cell Press},
  address   = {Cambridge},
  issn      = {1534-5807},
  doi       = {10.1016/j.devcel.2017.10.017},
  pages     = {290 -- +},
  year      = {2017},
  abstract  = {The epidermis of aerial plant organs is thought to be limiting for growth, because it acts as a continuous load-bearing layer, resisting tension. Leaf epidermis contains jigsaw puzzle piece-shaped pavement cells whose shape has been proposed to be a result of subcellular variations in expansion rate that induce local buckling events. Paradoxically, such local compressive buckling should not occur given the tensile stresses across the epidermis. Using computational modeling, we show that the simplest scenario to explain pavement cell shapes within an epidermis under tension must involve mechanical wall heterogeneities across and along the anticlinal pavement cell walls between adjacent cells. Combining genetics, atomic force microscopy, and immunolabeling, we demonstrate that contiguous cell walls indeed exhibit hybrid mechanochemical properties. Such biochemical wall heterogeneities precede wall bending. Altogether, this provides a possible mechanism for the generation of complex plant cell shapes.},
  language  = {en}
}
@article{LiuVainViottietal.2018,
  author    = {Liu, Qinsong and Vain, Thomas and Viotti, Corrado and Doyle, Siamsa M. and Tarkowska, Danuse and Novak, Ondrej and Zipfel, Cyril and Sitbon, Folke and Robert, Stephanie and Hofius, Daniel},
  title     = {Vacuole integrity maintained by DUF300 proteins is required for brassinosteroid signaling regulation},
  series = {Molecular plant},
  volume    = {11},
  journal   = {Molecular plant},
  number    = {4},
  publisher = {Cell Press},
  address   = {Cambridge},
  issn      = {1674-2052},
  doi       = {10.1016/j.molp.2017.12.015},
  pages     = {553 -- 567},
  year      = {2018},
  abstract  = {Brassinosteroid (BR) hormone signaling controls multiple processes during plant growth and development and is initiated at the plasma membrane through the receptor kinase BRASSINOSTEROID INSENSITIVE1 (BRI1) together with co-receptors such as BRI1-ASSOCIATED RECEPTOR KINASE1 (BAK1). BRI1 abundance is regulated by endosomal recycling and vacuolar targeting, but the role of vacuole-related proteins in BR receptor dynamics and BR responses remains elusive. Here, we show that the absence of two DUF300 domain-containing tonoplast proteins, LAZARUS1 (LAZ1) and LAZ1 HOMOLOG1 (LAZ1H1), causes vacuole morphology defects, growth inhibition, and constitutive activation of BR signaling. Intriguingly, tonoplast accumulation of BAK1 was substantially increased and appeared causally linked to enhanced BRI1 trafficking and degradation in laz1 laz1h1 plants. Since unrelated vacuole mutants exhibited normal BR responses, our findings indicate that DUF300 proteins play distinct roles in the regulation of BR signaling by maintaining vacuole integrity required to balance subcellular BAK1 pools and BR receptor distribution.},
  language  = {en}
}
@article{DejongheKuenenMylleetal.2016,
  author    = {Dejonghe, Wim and Kuenen, Sabine and Mylle, Evelien and Vasileva, Mina and Keech, Olivier and Viotti, Corrado and Swerts, Jef and Fendrych, Matyas and Ortiz-Morea, Fausto Andres and Mishev, Kiril and Delang, Simon and Scholl, Stefan and Zarza, Xavier and Heilmann, Mareike and Kourelis, Jiorgos and Kasprowicz, Jaroslaw and Nguyen, Le Son Long and Drozdzecki, Andrzej and Van Houtte, Isabelle and Szatmari, Anna-Maria and Majda, Mateusz and Baisa, Gary and Bednarek, Sebastian York and Robert, Stephanie and Audenaert, Dominique and Testerink, Christa and Munnik, Teun and Van Damme, Daniel and Heilmann, Ingo and Schumacher, Karin and Winne, Johan and Friml, Jiri and Verstreken, Patrik and Russinova, Eugenia},
  title     = {Mitochondrial uncouplers inhibit clathrin-mediated endocytosis largely through cytoplasmic acidification},
  series = {Nature Communications},
  volume    = {7},
  journal   = {Nature Communications},
  publisher = {Nature Publ. Group},
  address   = {London},
  issn      = {2041-1723},
  doi       = {10.1038/ncomms11710},
  pages     = {1959 -- 1968},
  year      = {2016},
  abstract  = {ATP production requires the establishment of an electrochemical proton gradient across the inner mitochondrial membrane. Mitochondrial uncouplers dissipate this proton gradient and disrupt numerous cellular processes, including vesicular trafficking, mainly through energy depletion. Here we show that Endosidin9 (ES9), a novel mitochondrial uncoupler, is a potent inhibitor of clathrin-mediated endocytosis (CME) in different systems and that ES9 induces inhibition of CME not because of its effect on cellular ATP, but rather due to its protonophore activity that leads to cytoplasm acidification. We show that the known tyrosine kinase inhibitor tyrphostinA23, which is routinely used to block CME, displays similar properties, thus questioning its use as a specific inhibitor of cargo recognition by the AP-2 adaptor complex via tyrosine motif-based endocytosis signals. Furthermore, we show that cytoplasm acidification dramatically affects the dynamics and recruitment of clathrin and associated adaptors, and leads to reduction of phosphatidylinositol 4,5-biphosphate from the plasma membrane.},
  language  = {en}
}