Chitin-induced dimerization activates a plant immune receptor |
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| Authors: | Liu Tingting Liu Zixu Song Chuanjun Hu Yunfei Han Zhifu She Ji Fan Fangfang Wang Jiawei Jin Changwen Chang Junbiao Zhou Jian-Min Chai Jijie |
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| Institution: | Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100730, China. |
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| Abstract: | Pattern recognition receptors confer plant resistance to pathogen infection by recognizing the conserved pathogen-associated molecular patterns. The cell surface receptor chitin elicitor receptor kinase 1 of Arabidopsis (AtCERK1) directly binds chitin through its lysine motif (LysM)-containing ectodomain (AtCERK1-ECD) to activate immune responses. The crystal structure that we solved of an AtCERK1-ECD complexed with a chitin pentamer reveals that their interaction is primarily mediated by a LysM and three chitin residues. By acting as a bivalent ligand, a chitin octamer induces AtCERK1-ECD dimerization that is inhibited by shorter chitin oligomers. A mutation attenuating chitin-induced AtCERK1-ECD dimerization or formation of nonproductive AtCERK1 dimer by overexpression of AtCERK1-ECD compromises AtCERK1-mediated signaling in plant cells. Together, our data support the notion that chitin-induced AtCERK1 dimerization is critical for its activation. |
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