Structural plant biology

Structural Biology & Cell Biology & Genetics

Plants are nature’s other successful experiment with multicellular life. We are interested in signaling and metabolic pathways that allow plants to grow and to develop. Our approach combines structural biology and biochemistry with cell biology and genetics in Arabidopsis.

Currently, we study how plant cells communicate with each other at their cell membrane, where they have evolved unique membrane receptor kinases. These receptors sense steroid and peptide hormones to orchestrate growth and development, to establish and maintain stem cell populations and to form plant organs and tissues. We have shown that these receptors require helper proteins for activation. We now want to obtain a molecular understanding of plant peptide hormone signaling and identify novel receptor complexes.

A second line of research is to understand how plants sense and store phosphate, an essential plant nutrient. We became interested in this topic by identifying a protein complex, which uses cytosolic ATP to generate long chains of inorganic polyphosphate, an important phosphate store in yeast. We have initiated a set of projects to test whether plants also make use of polyphosphates to store phosphate.

Recent Publications

  • Plant photoreceptors and their signaling components compete for COP1 binding via VP peptide motifs
    Lau, K; Podolec, R; Chappuis, R; Ulm, R; Hothorn, M
    EMBO JOURNAL, 10.15252/embj.2019102140 
  • Crystal structure of the leucine-rich repeat ectodomain of the plant immune receptor kinase SOBIR1
    Hohmann, U; Hothorn, M
    ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 75 488-497; 10.1107/S2059798319005291 5 MAY 2019
  • Crystal structure of the pseudoenzyme PDX1.2 in complex with its cognate enzyme PDX1.3: a total eclipse
    Robinson, GC; Kaufmann, M; Roux, C; Martinez-Font, J; Hothorn, M; Thore, S; Fitzpatrick, TB
    ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 75 400-415; 10.1107/S2059798319002912 4 APR 2019
  • Concerted expression of a cell cycle regulator and a metabolic enzyme from a bicistronic transcript in plants
    Lorenzo-Orts, L; Witthoeft, J; Deforges, J; Martinez, J; Loubery, S; Placzek, A; Poirier, Y; Hothorn, LA; Jaillais, Y; Hothorn, M
    NATURE PLANTS, 5 (2):184-+; 10.1038/s41477-019-0358-3 FEB 2019
  • MacroH2A histone variants limit chromatin plasticity through two distinct mechanisms
    Kozlowski, M; Corujo, D; Hothorn, M; Guberovic, I; Mandemaker, IK; Blessing, C; Sporn, J; Gutierrez-Triana, A; Smith, R; Portmann, T; Treier, M; Scheffzek, K; Huet, S; Timinszky, G; Buschbeck, M; Ladurner, AG
    EMBO REPORTS, 19 (10):10.15252/embr.201744445 OCT 2018
  • CLERK is a novel receptor kinase required for sensing of root-active CLE peptides in Arabidopsis
    Anne, Pauline; Amiguet-Vercher, Amelia; Brandt, Benjamin; Kalmbach, Lothar; Geldner, Niko; Hothorn, Michael; Hardtke, Christian S
    DEVELOPMENT   Volume: 145   Issue: 10     Article Number: UNSP dev162354 MAY 2018
  • The SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signalling
    Ulrich Hohmann, Joël Nicolet, Andrea Moretti, Ludwig A. Hothorn & Michael Hothorn
    Nature Plants (2018),
  • Mechanistic basis for the activation of plant membrane receptor kinases by SERK-family coreceptors
    Hohmann, U; Santiago, J; Nicolet, J; Olsson, V; Spiga, FM; Hothorn, LA; Butenko, MA; Hothorn, M
  • Control of plant phosphate homeostasis by inositol pyrophosphates and the SPX domain 
    Jung, Ji-Yul; Ried, Martina K.; Hothorn, Michael; et al. 
  • Perception of root-active CLE peptides requires CORYNE function in the phloem vasculature 
    Hazak, Ora; Brandt, Benjamin; Cattaneo, Pietro; Santiago, J; Rodriguez-Villalon, A; Hothorn, M; Hardtke, CS
    EMBO REPORTS, 18 (8): 1367-1381 AUG 2017
  • The Structural Basis of Ligand Perception and Signal Activation by Receptor Kinases 
    Hohmann, Ulrich; Lau, Kelvin; Hothorn, Michael 
    ANNUAL REVIEW OF PLANT BIOLOGY, VOL 68, 68: 109-137 2017 Review; Book Chapter (Details)
  • The macro domain as fusion tag for carrier-driven crystallization 
    Wild, Rebekka; Hothorn, Michael 
    PROTEIN SCIENCE, 26 (2): 365-374 FEB 2017 Document Type: Article (Details)
  • Control of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domains 
    Wild, Rebekka; Gerasimaite, Ruta; Jung, Ji-Yul; et al. 
    SCIENCE, 352 (6288): 986-990 MAY 20 2016 Document Type: Article (Details)
Michael Hothorn Univ Geneva

Prof. Dr. Michael Hothorn
University of Geneva
Department of Botany and Plant Biology
1211 Geneva

Tel: +41 (0)22 379 30 13

Research topics

  • Plant membrane signaling
  • Receptor kinases
  • Brassinosteroid signaling
  • Cytokinin signaling
  • Polyphosphate metabolism
  • Phosphate sensing



  • Receptor agonist/antagonist development
  • Structural Biology / Protein Crystallography of signaling proteins and metabolic enzymes
  • Quantitative biochemistry. Protein-Protein interactions. Protein-Ligand interactions