Chitin is a fungal microbe-associated molecular pattern recognized in Arabidopsis by a lysin motif receptor kinase (LYK), AtCERK1. Previous research suggested that AtCERK1 is the major chitin receptor and mediates chitin-induced signaling through homodimerization and phosphorylation. However, the reported chitin binding affinity of AtCERK1 is quite low, suggesting another receptor with high chitin binding affinity might be present. Here, we propose that AtLYK5 is the primary chitin receptor in Arabidopsis. Mutations in AtLYK5 resulted in a significant reduction in chitin response. However, AtLYK5 shares overlapping function with AtLYK4 and, therefore, Atlyk4/Atlyk5-2 double mutants show a complete loss of chitin response. AtLYK5 interacts with AtCERK1 in a chitin-dependent manner. Chitin binding to AtLYK5 is indispensable for chitin-induced AtCERK1 phosphorylation. AtLYK5 binds chitin at a much higher affinity than AtCERK1. The data suggest that AtLYK5 is the primary receptor for chitin, forming a chitin inducible complex with AtCERK1 to induce plant immunity.
Invading fungi are responsible for many of the plant diseases that affect global crop production. Plants have to be able to identify these fungi, and activate the right defense strategies if they are to protect themselves. Chitin is a polymer that is found in the cell walls of all fungi, but not in plants, so if the plant detects chitin, it knows that a potentially harmful fungus may be nearby.
The detection of chitin, and the resulting activation of a plant's defenses, requires a receptor protein called CERK1. In rice, CERK1 needs to interact with another receptor protein called CEBiP, which binds to chitin. However, in Arabidopsis thaliana—which is widely studied in plant research—CERK1 can bind to chitin on its own, although this interaction is very weak, so it has been suggested that a second protein may be involved.
Cao et al. have now found that a receptor protein called LYK5, which is very similar to CERK1, is much better at attaching to chitin in A. thaliana. It can also bind to CERK1, but only when chitin is present, and is required for activation of basic plant defenses. The experiments suggest that LYK5 detects chitin on behalf of CERK1, in a similar way to how CEBiP works in rice.
The next step in this research is to work out how CERK1 and LYK5 are able to activate plant defenses.