机构地区:[1]Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua Uni- versity, Beijing 100084, China [2]The State Key Laboratory of Protein and Plant Gene Research, Peking-Tsinghua Joint Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, College of Life Sciences, Peking University, Beijing 100871, China [3]Department of Biology, South University of Science and Technology of China, Shenzhen, Guangdong 518055, China
出 处:《Cell Research》2016年第6期674-685,共12页细胞研究(英文版)
基 金:Acknowledgments We thank S Huang and J He at Shanghai Synchrotron Radiation Facility (SSRF) for assistance with data collection; H Deng and J Liu at the center for Biomedical Analysis of Tsinghua University for MS analysis; L Li and A Jiang at Peking University for pro- viding the incubator. We acknowledge the Tsinghua University Branch of China National Center for Protein Sciences Beijing for providing the facility support. This work was funded by Projects of International Cooperation and Exchanges of the National Natural Science Foundation of China (31420103906), the Ministry of Science and Technology of China (2015CB910200) and State Key Program of the National Natural Science of China (31130063 and 31421001) to JC; the National Natural Science Foundation of Chi- na (91217305 and 91017010) to HG.
摘 要:Peptide-mediated cell-to-cell signaling has crucial roles in coordination and definition of cellular functions in plants. Peptide-receptor matching is important for understanding the mechanisms underlying peptide-mediated sig- naling. Here we report the structure-guided identification of root meristem growth factor (RGF) receptors important for plant development. An assay based on a signature ligand recognition motif (Arg-x-Arg) conserved in a subfamily of leucine-rich repeat receptor kinases CLRR-RKs) identified the functionally uncharacterized LRR-RK At4926540 as a receptor of RGF1 (RGFR1). We further solved the crystal structure of RGF1 in complex with the LRR domain of RGFR1 at a resolution of 2.6 A, which reveals that the Arg-x-Gly-Gly (RxGG) motif is responsible for specific rec- ognition of the sulfate group of RGF1 by RGFR1. Based on the RxGG motif, we identified additional four RGFRs. Participation of the five RGFRs in RGF-induced signaling is supported by biochemical and genetic data. We also of- fer evidence showing that SERKs function as co-receptors for RGFs. Taken together, our study identifies RGF receptors and co-receptors that can link RGF signals with their downstream components and provides a proof of principle for structure-based matching of LRR-RKs with their peptide ligands.
关 键 词:peptide hormone RAM RGF receptor crystal structure RxR motif
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