Difference between revisions of "Os09g0511000"
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''OsCERK1'' encoded a receptor-like kinase consisting of 624 amino acid residues, containing a signal peptide, an extracellular domain, a transmembrane region and an intracellular Ser/Thr kinase domain (Figure 1). [[File:F 1.png|thumb|Figure 1 Amino acid sequence of OsCERK1 predicted from the cDNA. Underlining indicates the sequence corresponding to the LysM motif. EC, extracellular domain; IC, intracellular domain; SP, signal peptide; TM, transmembrane domain.]] OsCERK1 is a plasma membrane protein containing one LysM motif in the extracellular domain and an intracellular Ser/Thr kinase domain. <ref name="ref 1" /> | ''OsCERK1'' encoded a receptor-like kinase consisting of 624 amino acid residues, containing a signal peptide, an extracellular domain, a transmembrane region and an intracellular Ser/Thr kinase domain (Figure 1). [[File:F 1.png|thumb|Figure 1 Amino acid sequence of OsCERK1 predicted from the cDNA. Underlining indicates the sequence corresponding to the LysM motif. EC, extracellular domain; IC, intracellular domain; SP, signal peptide; TM, transmembrane domain.]] OsCERK1 is a plasma membrane protein containing one LysM motif in the extracellular domain and an intracellular Ser/Thr kinase domain. <ref name="ref 1" /> | ||
====OsCERK1 is essential for chitin elicitor signaling in rice cells==== | ====OsCERK1 is essential for chitin elicitor signaling in rice cells==== | ||
| − | Knockdown of ''OsCERK1'' resulted in a marked suppression of the defense responses in rice cells induced by chitin oligosaccharides, indicating a central role for OsCERK1 in chitin signaling in rice. The results of yeast two-hybrid assay indicate that the extracellular domain of OsCERK1 can interact with that of CEBiP, suggesting that OsCERK1 and CEBiP have the potential to form homo- and hetero-oligomers through interaction of their LysM-containing extracellular domains. < | + | Knockdown of ''OsCERK1'' resulted in a marked suppression of the defense responses in rice cells induced by chitin oligosaccharides, indicating a central role for OsCERK1 in chitin signaling in rice. The results of yeast two-hybrid assay indicate that the extracellular domain of OsCERK1 can interact with that of CEBiP, suggesting that OsCERK1 and CEBiP have the potential to form homo- and hetero-oligomers through interaction of their LysM-containing extracellular domains. <ref name="ref 1" /> |
These results indicated that, in the absence of chitin oligosaccharide elicitor, a major portion of CEBiP exists most likely as homo-oligomers in the plasma membrane, whereas OsCERK1 is mostly present as a monomer. However, when the chitin oligosaccharide elicitor is added to the cells, a portion of CEBiP and OsCERK1 appear to form a hetero-oligomer receptor complex. <ref name="ref 1" /> | These results indicated that, in the absence of chitin oligosaccharide elicitor, a major portion of CEBiP exists most likely as homo-oligomers in the plasma membrane, whereas OsCERK1 is mostly present as a monomer. However, when the chitin oligosaccharide elicitor is added to the cells, a portion of CEBiP and OsCERK1 appear to form a hetero-oligomer receptor complex. <ref name="ref 1" /> | ||
Other researchers also confirm that these two proteins form a receptor complex that transduces the chitin signal to downstream components for immune responses. <ref name="ref 2" /> <ref name="ref 3" /> <ref name="ref 4" /> | Other researchers also confirm that these two proteins form a receptor complex that transduces the chitin signal to downstream components for immune responses. <ref name="ref 2" /> <ref name="ref 3" /> <ref name="ref 4" /> | ||
====OsCERK1 signal pathway==== | ====OsCERK1 signal pathway==== | ||
| − | OsRacGEF1 as a guanine nucleotide exchange factor for OsRac1 (rice small GTPase). OsRacGEF1 interacts with OsCERK1 and is activated when its C-terminal S549 is phosphorylated by the cytoplasmic domain of OsCERK1 in response to chitin. Activated OsRacGEF1 is required for chitin-driven immune responses and resistance to rice blast fungus infection. Further, a protein complex including OsCERK1 and OsRacGEF1 is transported from the endoplasmic reticulum to the PM. OsCEBiP, OsCERK1, OsRacGEF1, and OsRac1 function as key components of a | + | OsRacGEF1 as a guanine nucleotide exchange factor for OsRac1 (rice small GTPase). OsRacGEF1 interacts with OsCERK1 and is activated when its C-terminal S549 is phosphorylated by the cytoplasmic domain of OsCERK1 in response to chitin. Activated OsRacGEF1 is required for chitin-driven immune responses and resistance to rice blast fungus infection. Further, a protein complex including OsCERK1 and OsRacGEF1 is transported from the endoplasmic reticulum to the PM. OsCEBiP, OsCERK1, OsRacGEF1, and OsRac1 function as key components of a ''defensome'' critically engaged early during chitin-induced immunity. <ref name="ref 6" /> |
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===Expression=== | ===Expression=== | ||
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===Evolution=== | ===Evolution=== | ||
Phylogenies were analyzed by multiple sequence alignment of the protein sequences of the LysM receptor-like kinases. The names of proteins described previously (Zhang et al., 2007) <ref name="ref 5" /> are shown in parentheses for ease of comparison. [[File:F 3.png|thumb|Figure 3 Phylogenetic tree of OsCERK1 and related plant LysM receptor-like kinases.]] The scale indicates the base substitution rate, and numbers at the nodes represent bootstrap values with 1000 replicates (Figure 3). <ref name="ref 1" /> | Phylogenies were analyzed by multiple sequence alignment of the protein sequences of the LysM receptor-like kinases. The names of proteins described previously (Zhang et al., 2007) <ref name="ref 5" /> are shown in parentheses for ease of comparison. [[File:F 3.png|thumb|Figure 3 Phylogenetic tree of OsCERK1 and related plant LysM receptor-like kinases.]] The scale indicates the base substitution rate, and numbers at the nodes represent bootstrap values with 1000 replicates (Figure 3). <ref name="ref 1" /> | ||
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==Labs working on this gene== | ==Labs working on this gene== | ||
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==Structured Information== | ==Structured Information== | ||
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[[Category:Genes]] | [[Category:Genes]] | ||
[[Category:Japonica mRNA]] | [[Category:Japonica mRNA]] | ||
Latest revision as of 13:15, 25 March 2017
The rice gene Os09g0511000 is known as OsCERK1. OsCERK1 encodes a receptor-like kinase called OsCERK1 which is essential for chitin elicitor signaling in rice cells.
Contents
Annotated Information
Function
OsCERK1 encoded a receptor-like kinase called OsCERK1
OsCERK1 encoded a receptor-like kinase consisting of 624 amino acid residues, containing a signal peptide, an extracellular domain, a transmembrane region and an intracellular Ser/Thr kinase domain (Figure 1). OsCERK1 is a plasma membrane protein containing one LysM motif in the extracellular domain and an intracellular Ser/Thr kinase domain. [1]
OsCERK1 is essential for chitin elicitor signaling in rice cells
Knockdown of OsCERK1 resulted in a marked suppression of the defense responses in rice cells induced by chitin oligosaccharides, indicating a central role for OsCERK1 in chitin signaling in rice. The results of yeast two-hybrid assay indicate that the extracellular domain of OsCERK1 can interact with that of CEBiP, suggesting that OsCERK1 and CEBiP have the potential to form homo- and hetero-oligomers through interaction of their LysM-containing extracellular domains. [1] These results indicated that, in the absence of chitin oligosaccharide elicitor, a major portion of CEBiP exists most likely as homo-oligomers in the plasma membrane, whereas OsCERK1 is mostly present as a monomer. However, when the chitin oligosaccharide elicitor is added to the cells, a portion of CEBiP and OsCERK1 appear to form a hetero-oligomer receptor complex. [1] Other researchers also confirm that these two proteins form a receptor complex that transduces the chitin signal to downstream components for immune responses. [2] [3] [4]
OsCERK1 signal pathway
OsRacGEF1 as a guanine nucleotide exchange factor for OsRac1 (rice small GTPase). OsRacGEF1 interacts with OsCERK1 and is activated when its C-terminal S549 is phosphorylated by the cytoplasmic domain of OsCERK1 in response to chitin. Activated OsRacGEF1 is required for chitin-driven immune responses and resistance to rice blast fungus infection. Further, a protein complex including OsCERK1 and OsRacGEF1 is transported from the endoplasmic reticulum to the PM. OsCEBiP, OsCERK1, OsRacGEF1, and OsRac1 function as key components of a defensome critically engaged early during chitin-induced immunity. [5]
Expression
OsCERK1 was expressed in all tissues tested, with weak expression in the flowers (Figure 2). [1]
Evolution
Phylogenies were analyzed by multiple sequence alignment of the protein sequences of the LysM receptor-like kinases. The names of proteins described previously (Zhang et al., 2007) [6] are shown in parentheses for ease of comparison. The scale indicates the base substitution rate, and numbers at the nodes represent bootstrap values with 1000 replicates (Figure 3). [1]
Labs working on this gene
- Department of Life Sciences, Faculty of Agriculture, Meiji University, 1-1-1 Higashi-Mita, Tama-ku, Kawasaki, Kanagawa 214-8571, Japan
- Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan
- Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan
- Laboratory of Plant Molecular Genetics, Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan
- Agricultural and Veterinary Research Laboratories, Meiji Seika Kaisha, Kohoku-ku, Yokohama 222–8567, Japan
References
- ↑ 1.0 1.1 1.2 1.3 1.4 Takeo Shimizu, Takuto Nakano and Daisuke Takamizawa et al. (2010) Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice. The Plant Journal, 64, 204–214
- ↑ Kaku, H., Nishizawa, Y., Ishii-Minami, N., Akimoto-Tomiyama, C., Dohmae, N., Takio, K., Minami, E., and Shibuya, N. (2006). Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor. Proc. Natl. Acad. Sci. USA103, 11086–11091.
- ↑ Shimizu, T., Nakano, T., Takamizawa, D., Desaki, Y., Ishii-Minami, N., Nishizawa, Y., Minami, E., Okada, K., Yamane, H., Kaku, H., and Shibuya, N. (2010). Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice. Plant J.64, 204–214.
- ↑ Shinya, T., Motoyama, N., Ikeda, A., Wada, M., Kamiya, K., Hayafune, M., Kaku, H., and Shibuya, N. (2012). Functional characterization of CEBiP and CERK1 homologs in arabidopsis and rice reveals the presence of different chitin receptor systems in plants. Plant Cell Physiol.53, 1696–1706.
- ↑ Akira Akamatsu, Hann Lin Wong and Masayuki Fujiwara et al. (2013) An OsCEBiP/OsCERK1-OsRacGEF1-OsRac1 Module Is an Essential Early Component of Chitin-Induced Rice Immunity. Cell Host & Microbe 13, 465–476
- ↑ Zhang, X.C., Wu, X., Findley, S., Wan, J., Libault, M., Nguyen, H.T., Cannon, S.B. and Stacey, G. (2007) Molecular evolution of lysin motif-type receptorlike kinases in plants. Plant Physiol.144, 623–636.
