Poster
Henriette Ruebsam
Faculty of Biology, University of Freiburg
Freiburg, Baden-Wurttemberg, Germany
Bine Simonsen
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Kira Gysel
Assistant Professor
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Simon B. Hansen
Department of Molecular Biology and Genetics, Aarhus University
Zürich, Zurich, Switzerland
Marie Vogel Kolte
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Maria Meisner Larsen
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Christina Kroenauer
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Maria Vinther
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Jens Stougaard
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Simona Radutoiu
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Kasper Andersen
Department of Molecular Biology and Genetics, Aarhus University
Aarhus, Midtjylland, Denmark
Plants perceive chitin derived from fungal cell walls through lysin motif (LysM) receptor kinases. In the model legume Medicago truncatula, the active kinase receptor CERK1 and the pseudokinase receptor LYR4 play crucial roles in chitin-triggered immunity signaling. Previous studies indicated size-selectivity in chitin perception, but the molecular basis remained unclear. We identified an additional N-terminal domain in the crystal structure of the LYR4 ectodomain, which enables the specific recognition of long chitin chains. Furthermore, structural and biochemical characterization of the LYR4 intracellular domain revealed phosphorylation activity despite the absence of canonical kinase features. Through binding studies and in planta experiments we demonstrated that LYR4 is the primary chitin binder in Medicago, but that reactive-oxygen species production is independent of its catalytic activity. We conclude that LYR4 rather serves as a scaffold for downstream signaling components and likely forms a complex with CERK1 upon chitin binding. These findings provide a mechanistic understanding of how plants specifically respond to chitin and initiate an immune response.