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.
- 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, * equal contribution
- Hothorn M*, Van den Ende W*, Lammens W, Rybin V, Scheffzek K (2010) Structural insights into the pH-controlled targeting of plant cell-wall invertase by a specific inhibitor protein. PNAS 107(4):17427-32, * equal contribution
- Hothorn M, Neumann H, Lenherr ED, Wehner M, Rybin V, Hassa PO, Uttenweiler A, Reinhardt M, Schmidt A, Seiler J, Ladurner AG, Herrmann C, Scheffzek K, Mayer A (2009) Catalytic core of a membrane-associated eukaryotic polyphosphate polymerase. Science 324(5926):513-6
The lab is currently based at the Friedrich Miescher Laboratory, located at the Max-Planck-Campus in Tuebingen, Germany.