Hothorn Lab: Structural Plant Biology

Signal perception at the cell surface and transduction of this signal to the cell's interior is essential to all life forms. Plants have evolved membrane-integral receptor proteins and associated signaling cascades that drastically differ from the well-studied systems in animals. Our aim is to dissect these signaling pathways in mechanistic detail.

Recent publications
  • Bojar D, Martinez J, Santiago J, Rybin V, Bayliss R, Hothorn M (2014) Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. Plant J doi: 10.1111/tpj.12445
  • Santiago J, Henzler C, Hothorn M (2013) Molecular Mechanism for Plant Steroid Receptor Activation by Somatic Embryogenesis Co-Receptor Kinases. Science  341:889-92
  • Christie JM, Arvai AS, Baxter KJ, Heilmann M, Pratt AJ, O'Hara A, Kelly SM, Hothorn M, Smith BO, Hitomi K, Jenkins GI, Getzoff ED (2012) Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated disruption of cross-dimer salt bridges. Science 335:1492-1496
  • Hothorn M, Dabi T, Chory J (2011) Structural basis for cytokinin recognition by Arabidopsis histidine kinase 4. Nature Chem Biol 7:766-68
  • Hothorn M, Belkhadir Y, Dreux M, Dabi T, Noel JP, Wilson IA, Chory J (2011) Structural basis of steroid hormone perception by the receptor kinase BRI1. Nature 474(7352):467-71
  • Jaillais Y, Hothorn M, Belkhadir Y, Dabi T, Nimchuk ZL, Meyerowitz EM, Chory J (2011) Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor. Genes Dev 25(3):232-7
Ongoing projects in the lab are supported by the Max Planck Society, by an European Research Council starting grant, by a Career Development Award from the Human Frontier Science Program (HFSP) Organisation, and by a FEBS postdoctoral fellowship (to Julia Santiago-Cuellar).