| Title | Chitin-Induced Dimerization Activates a Plant Immune Receptor |
| 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 |
| Affiliation | Zhengzhou Univ, Dept Chem, Zhengzhou 450001, Peoples R China. Chinese Acad Med Sci, Grad Program, Beijing 100730, Peoples R China. Peking Union Med Coll, Beijing 100730, Peoples R China. Tsinghua Peking Ctr Life Sci, Beijing 100084, Peoples R China. Tsinghua Univ, Sch Life Sci, Beijing 100084, Peoples R China. Natl Inst Biol Sci, Beijing 102206, Peoples R China. Nanjing Univ, Sch Life Sci, Nanjing 210093, Peoples R China. Peking Univ, Beijing NMR Ctr, Beijing 100871, Peoples R China. Peking Univ, Coll Life Sci, Beijing 100871, Peoples R China. Chinese Acad Sci, Inst Genet & Dev Biol, State Key Lab Plant Genom, Beijing 100101, Peoples R China. Chinese Acad Sci, Inst Genet & Dev Biol, Natl Ctr Plant Gene Res, Beijing 100101, Peoples R China. |
| Keywords | PATTERN-RECOGNITION RECEPTORS ARABIDOPSIS-THALIANA INNATE IMMUNITY KINASE LYSM BINDING DEFENSE PERCEPTION RESISTANCE PROTEINS |
| Issue Date | 2012 |
| Publisher | science |
| Citation | SCIENCE.2012,336,(6085),1160-1164. |
| 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. |
| URI | http://hdl.handle.net/20.500.11897/393466 |
| ISSN | 0036-8075 |
| DOI | 10.1126/science.1218867 |
| Indexed | SCI(E) |
| Appears in Collections: | 生命科学学院 |
