The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The target is the japonica rice protein OsCERK1, UniProt A0A0P0XII1, encoded by CERK1/OsLysM-RLK9 (the supplied record also lists Os08g0538300 and LOC_Os08g42580). This assignment matches the rice protein called OsLysM-RLK9 in the original characterization; it is not Arabidopsis CERK1, whose chitin-binding behavior differs. The experimentally characterized rice protein has 624 amino acids, an N-terminal signal peptide, an extracellular LysM-containing region, one transmembrane segment and an intracellular serine/threonine kinase domain. Motif analysis identified one recognizable extracellular LysM motif in rice OsCERK1, versus three in the Arabidopsis protein. The locus identifiers above come from the UniProt information supplied with the question; the cited characterization independently establishes the OsLysM-RLK9/OsCERK1 name and protein architecture. (shimizu2010twolysmreceptor pages 1-2, shimizu2010twolysmreceptor pages 2-3, shinya2012functionalcharacterizationof pages 3-4)
Primary annotation: OsCERK1 is a plasma-membrane receptor-like kinase and shared signaling component of two rice pathways: chitin-triggered innate immunity and perception of arbuscular-mycorrhizal fungal signals. Its main biochemical activity is transfer of phosphate from ATP to protein substrates, including OsRacGEF1, OsRLCK185, OsMYR1 and OsCIE1; it also autophosphorylates. It is not a chitin-degrading enzyme or a transporter. Nor should its participation in chitin perception be equated with proven high-affinity direct chitin binding: in the tested colloidal-chitin assay, the rice OsCERK1 ectodomain did not bind, whereas partner receptors provide directly demonstrated ligand binding. Detailed catalytic constants or a complete physiological substrate repertoire have not been established by the studies examined. (shinya2012functionalcharacterizationof pages 3-4, he2019alysmreceptor pages 7-10, akamatsu2013anoscebiposcerk1osracgef1osrac1module pages 1-2, yamaguchi2013areceptorlikecytoplasmic pages 1-2, wang2024releaseofa pages 4-5)
OsCERK1 spans the plasma membrane: its LysM-containing region faces the extracellular space and its catalytic domain faces the cytoplasm. Rice root epidermal and cortical expression, plasma-membrane localization and membrane-localized interaction with OsMYR1 support its role at the plant–microbe interface; plasma-membrane experiments also place its immune signaling partners there. Evidence that an OsCERK1–OsRacGEF1 complex traffics from the endoplasmic reticulum to the plasma membrane describes receptor delivery, not the ER as its principal signaling site. (shimizu2010twolysmreceptor pages 2-3, he2019alysmreceptor pages 7-10, akamatsu2013anoscebiposcerk1osracgef1osrac1module pages 2-3, akamatsu2013anoscebiposcerk1osracgef1osrac1module pages 1-2)
In the immune complex, extracellular fungal chitin fragments—particularly longer chitooligosaccharides such as the eight-residue CO8, or (GlcNAc)₈—are bound principally by OsCEBiP. Chitin-oligosaccharide treatment promotes formation of an OsCEBiP–OsCERK1 membrane complex. Binding of labeled chitin oligomer to rice membranes persisted after OsCERK1 knockdown, while an isolated OsCERK1 ectodomain failed to bind colloidal chitin under the conditions tested. These are stronger grounds for annotating OsCERK1 as the kinase-bearing signaling partner than as a directly proven high-affinity CO8-binding protein. A negative result in that assay does not exclude every possible weak or context-dependent interaction. Rice and Arabidopsis results must not be interchanged: the latter protein's direct chitin binding does not establish the same property for OsCERK1. (shimizu2010twolysmreceptor pages 1-2, shimizu2010twolysmreceptor pages 3-4, shinya2012functionalcharacterizationof pages 3-4, shinya2012functionalcharacterizationof pages 5-7)
In the symbiotic complex, OsMYR1/OsLYK2 directly recognizes the short fungal chitooligosaccharide CO4 (chitotetraose). Its purified ectodomain bound CO4 with a measured Kᵈ of 89 ± 44.9 nM; CO4 increased OsMYR1–OsCERK1 association approximately twofold. OsMYR1 also interacted with long-chain chitin beads, with CO4 and CO8 competing for that association. Thus, CO length helps bias the response, but CO4-versus-CO8 sensing is not an absolute, one-ligand/one-receptor rule. The quoted affinity is for OsMYR1, not OsCERK1, and should not be assigned to the target kinase. (he2019alysmreceptor pages 7-10, zhang2021discriminatingsymbiosisand pages 1-2)
The supported reaction class is ATP-dependent phosphorylation of a protein serine or threonine residue: protein–OH + ATP → protein–O–phosphate + ADP. This formulation specifies OsCERK1's phosphotransfer role, not specificity for one small-molecule substrate. Purified OsCERK1 kinase domain autophosphorylated and phosphorylated OsMYR1 and the assay substrate myelin basic protein; the OsCERK1 T484A activation-loop variant lacked detectable kinase activity in vitro. OsMYR1 did not show comparable intrinsic kinase activity, helping explain why the ligand-binding symbiotic receptor recruits OsCERK1. CO4 enhanced phosphorylation of the receptor pair in cells and transgenic rice. (he2019alysmreceptor pages 7-10)
Several protein substrates and downstream branches have more precise experimental support:
The following table consolidates the rice-specific ligand, localization, phosphorylation and perturbation evidence; it separates what binds extracellular ligand from what catalyzes intracellular signaling. (shimizu2010twolysmreceptor pages 2-3, he2019alysmreceptor pages 7-10)
| Mode / partner | Ligand or substrate | Direct rice-specific evidence / readout | Key study, date, DOI / URL |
|---|---|---|---|
| Receptor topology and localization | — | OsCERK1 is a 624-aa, single-pass receptor-like kinase with an N-terminal signal peptide, extracellular LysM-containing region, transmembrane helix and intracellular Ser/Thr kinase domain. It is expressed broadly and localizes to the plasma membrane, including root epidermal and cortical cells. (shimizu2010twolysmreceptor pages 2-3, he2019alysmreceptor pages 7-10) | Shimizu et al., Sep 2010, 10.1111/j.1365-313X.2010.04324.x; He et al., Dec 2019, 10.1016/j.molp.2019.10.015 |
| Immunity: OsCEBiP–OsCERK1 | Long-chain chitin oligosaccharides, especially CO8 / (GlcNAc)₈ | OsCEBiP is the principal ligand-binding component; ligand treatment promotes an OsCEBiP–OsCERK1 complex. OsCERK1 knockdown markedly reduced biphasic ROS, phytoalexins and defense transcription: about 85% of normally upregulated and 98% of downregulated elicitor-responsive genes lost responsiveness. Importantly, the isolated OsCERK1 ectodomain did not bind colloidal chitin in the 2012 assay. (shimizu2010twolysmreceptor pages 1-2, shimizu2010twolysmreceptor pages 2-3, shinya2012functionalcharacterizationof pages 3-4, shinya2012functionalcharacterizationof pages 5-7, shimizu2010twolysmreceptor pages 3-4) | Shimizu et al., Sep 2010, 10.1111/j.1365-313X.2010.04324.x; Shinya et al., Oct 2012, 10.1093/pcp/pcs113 |
| Mycorrhiza: OsMYR1/OsLYK2–OsCERK1 | CO4 (chitotetraose); OsMYR1 also recognizes CO8 | OsMYR1 directly bound CO4 with Kᵈ = 89 ± 44.9 nM; CO4 increased OsMYR1–OsCERK1 association about twofold and enhanced receptor phosphorylation. CO4 induced nuclear Ca²⁺ oscillations in 42.8% of wild-type atrichoblasts versus 2.5% in Oscerk1-1 and 4% in Osmyr1-1. Kinase-dead OsCERK1-T484A failed to rescue mycorrhizal colonization. (he2019alysmreceptor pages 7-10, he2019alysmreceptor media 9c58ef8b) | He et al., Dec 2019, 10.1016/j.molp.2019.10.015 |
| Kinase substrate: OsRacGEF1 | OsRacGEF1 Ser549 | OsCERK1’s cytoplasmic domain phosphorylated OsRacGEF1 at Ser549, activating the GEF–OsRac1 branch at the plasma membrane; chitin-triggered OsRac1 activity was followed by a FRET biosensor at three-minute intervals. (akamatsu2013anoscebiposcerk1osracgef1osrac1module pages 1-2, akamatsu2013anoscebiposcerk1osracgef1osrac1module pages 2-3) | Akamatsu et al., Apr 2013, 10.1016/j.chom.2013.03.007 |
| Kinase substrate: OsRLCK185 | OsRLCK185 | Association and in-vitro kinase assays showed direct OsCERK1-dependent phosphorylation of OsRLCK185 at the plasma membrane. Silencing OsRLCK185 impaired chitin- and peptidoglycan-induced MAPK activation and defense-gene expression; OsRLCK185 relays signaling through OsMAPKKKε–OsMKK4–OsMPK3/6. (yamaguchi2013areceptorlikecytoplasmic pages 1-2, wang2017oscerk1mediatedchitinperception pages 1-5, wang2017oscerk1mediatedchitinperception pages 5-9) | Yamaguchi et al., Mar 2013, 10.1016/j.chom.2013.02.007; Wang et al., Apr 2017, 10.1016/j.molp.2017.01.006 |
| Kinase substrate: OsMYR1 | Kinase-inactive OsMYR1 intracellular domain | Purified OsCERK1 kinase phosphorylated itself, myelin basic protein and OsMYR1; OsMYR1 lacked detectable intrinsic kinase activity. CO4 enhanced phosphorylation of both receptors in protoplasts and transgenic rice. (he2019alysmreceptor pages 7-10) | He et al., Dec 2019, 10.1016/j.molp.2019.10.015 |
| Kinase substrate: OsCIE1 | OsCIE1 Thr206, Thr215, Thr216 and Ser237; principal regulatory site Ser237 | Chitin-activated OsCERK1 phosphorylates the U-box E3 ligase OsCIE1. Ser237 phosphorylation weakens OsCIE1–OsUBC8 association and suppresses E3 activity, releasing inhibition of OsCERK1. Phosphomimetic S237D showed reduced ubiquitination activity and failed to restore normal blast susceptibility fully. (wang2024releaseofa pages 4-5, wang2024releaseofa pages 5-6) | Wang et al., May 2024, 10.1038/s41586-024-07418-9 |
| Basal ubiquitin brake: OsCIE1→OsCERK1 | OsCERK1 Lys329, Lys347, Lys352, Lys445, Lys453, Lys458, Lys548, Lys558, Lys570 and Lys584 | In resting cells, OsCIE1 polyubiquitinates OsCERK1 at ten mapped lysines and inhibits kinase activity without promoting proteasomal degradation. Oscie1 mutants had stronger chitin-induced ROS and resistance to Magnaporthe oryzae and Xanthomonas oryzae, but reduced seed setting, grain yield and mycorrhizal colonization; double-mutant evidence showed substantial OsCERK1 dependence. (wang2024releaseofa pages 4-5, wang2024releaseofa pages 2-3, wang2024releaseofa pages 1-2) | Wang et al., May 2024, 10.1038/s41586-024-07418-9 |
| Experimental application: chitin-induced systemic resistance | Soil-applied chitin oligomers (DP2–6) or chitin nanofiber at 0.01–0.1% | Both preparations induced systemic resistance to Bipolaris oryzae and altered leaf cell-wall biogenesis; disruption of either OsCERK1 or OsCEBiP compromised the response. This was a controlled rice experiment, not yet evidence of routine field deployment. (takagi2022chitininducedsystemicdisease pages 1-2, takagi2022chitininducedsystemicdisease pages 2-3, takagi2022chitininducedsystemicdisease pages 11-12) | Takagi et al., Nov 2022, 10.3389/fpls.2022.1064628 |
| Experimental application: receptor competition | CO4 versus CO8 | OsMYR1–CO4 competes with OsCEBiP for OsCERK1, suppressing OsCERK1 homodimerization and OsGEF1 phosphorylation; conversely, OsCEBiP limits the symbiotic receptor complex. Osmyr1 mutants were more blast-resistant in roots, whereas early AM colonization increased in Oscebip. (zhang2021discriminatingsymbiosisand pages 1-2, zhang2021discriminatingsymbiosisand pages 2-3, zhang2021discriminatingsymbiosisand pages 4-5, zhang2021discriminatingsymbiosisand pages 3-4) | Zhang et al., Apr 2021, 10.1073/pnas.2023738118 |
Table: Rice-specific evidence distinguishes OsCERK1’s kinase/coreceptor function from direct ligand binding and summarizes its immune, mycorrhizal and ubiquitin-regulatory mechanisms. Quantitative findings and practical experiments are linked to primary studies.
Receptor competition provides an experimentally supported explanation for how one kinase can participate in opposing outcomes. In rice roots, OsMYR1 and OsCEBiP compete for OsCERK1: CO4/OsMYR1 favors the symbiotic receptor complex and reduces formation of the OsCEBiP–OsCERK1 immune complex. OsMYR1 also reduced OsCERK1 self-association and inhibited OsCERK1 autophosphorylation and phosphorylation of OsGEF1/OsRacGEF1 in vitro. Importantly, under the tested conditions it did not prevent phosphorylation of OsRLCK185; the competition model is therefore more nuanced than global shutdown of all OsCERK1 catalysis. Conversely, OsCEBiP impeded OsMYR1–OsCERK1 association. Osmyr1 mutants were more resistant to root infection by the rice-blast fungus Magnaporthe oryzae, whereas Oscebip showed increased early, but not persistently increased, arbuscular-mycorrhizal colonization. These results identify receptor-partner availability, ligand context and tissue as determinants of output. (zhang2021discriminatingsymbiosisand pages 1-2, zhang2021discriminatingsymbiosisand pages 2-3, zhang2021discriminatingsymbiosisand pages 4-5, zhang2021discriminatingsymbiosisand pages 5-6)
A May 2024 Nature primary study identified OsCIE1, a U-box E3 ubiquitin ligase, as a negative regulator of OsCERK1. In the basal state OsCIE1 ubiquitinates OsCERK1 and restrains its kinase activity without primarily driving proteasomal receptor degradation. Mass spectrometry identified ten modified OsCERK1 lysines: K329, K347, K352, K445, K453, K458, K548, K558, K570 and K584. Upon chitin activation, OsCERK1 phosphorylates OsCIE1 at several mapped positions, including the key Ser237 within its U-box region. This weakens recruitment of the E2 enzyme OsUBC8, suppresses OsCIE1's ubiquitin-ligase activity and releases the brake on immune signaling. Phosphorylation-mimicking OsCIE1 mutants supported that direction of causality. (wang2024releaseofa pages 4-5, wang2024releaseofa pages 2-3, wang2024releaseofa pages 5-6)
The genetic results expose an application-relevant constraint: Oscie1 mutants displayed stronger chitin-induced reactive-oxygen responses and increased resistance to M. oryzae and bacterial blight agent Xanthomonas oryzae pv. oryzae, but lower seed setting and grain yield, as well as reduced mycorrhizal colonization. Double-mutant evidence showed that much of this phenotype depends on OsCERK1. Consequently, simply maximizing OsCERK1 signaling is not a demonstrated yield-neutral crop-improvement strategy. (wang2024releaseofa pages 2-3, wang2024releaseofa pages 1-2)
Chitin treatment illustrates potential use of this receptor pathway rather than established routine deployment. In a November 2022 rice experiment, soil amended with chitin oligomers or chitin nanofibers at 0.01–0.1% induced systemic resistance in leaves to Bipolaris oryzae; disruption of either OsCERK1 or OsCEBiP compromised the effect. Leaf transcriptomic, cytokinin and cell-wall analyses implicated altered cell-wall biogenesis, but the root-to-leaf signal and direct perception of nanofibers were not identified. Thus the study supports an experimental elicitor strategy, not a defined OsCERK1-mediated nanofiber-binding reaction or proven field-level benefit. (takagi2022chitininducedsystemicdisease pages 1-2, takagi2022chitininducedsystemicdisease pages 2-3, takagi2022chitininducedsystemicdisease pages 11-12, takagi2022chitininducedsystemicdisease pages 5-6)
Breeding and mycorrhiza management require cultivar-specific evaluation. A September 2024 review discusses naturally varying OsCERK1 alleles associated with mycorrhizal performance and blast resistance and notes that an additional proposed LCO receptor, OsLYK11, is present in one examined rice genotype but absent from the examined japonica genome. OsLYK11 is another gene, not an alternative name for the japonica OsCERK1 studied here; differences among cultivars and ligand classes prevent assuming that all rice lines share the same symbiotic receptor complement. A contemporaneous 2024 preprint investigated other LysM-receptor groups across plants, but its non-OsCERK1 ligand-binding measurements should not be substituted for measurements on this protein. These findings motivate receptor-allele and agronomic testing rather than establish an implemented OsCERK1-based cultivar improvement for this UniProt entry. (he2024agapin pages 2-3, ding2024anewgroup pages 1-4)
Overall assessment. The strongest functional annotation is a plasma-membrane, ATP-dependent LysM receptor-like protein kinase that transduces chitin-associated immune signals with OsCEBiP and CO4-associated mycorrhizal signals with OsMYR1. Direct rice experiments establish receptor-partner interactions, defined phosphorylation events, loss-of-function phenotypes and the 2024 OsCIE1 regulatory mechanism. Precise ligand affinity for OsCERK1 itself, full substrate-site specificity, how nuclear calcium signaling is coupled molecularly to this kinase, and yield-neutral manipulation of its immune–symbiotic balance remain insufficiently resolved. (shimizu2010twolysmreceptor pages 1-2, shinya2012functionalcharacterizationof pages 3-4, he2019alysmreceptor pages 7-10, wang2024releaseofa pages 4-5, wang2024releaseofa pages 2-3)
References
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(he2019alysmreceptor media 9c58ef8b): Jiangman He, Chi Zhang, Huiling Dai, Huan Liu, Xiaowei Zhang, Jun Yang, Xi Chen, Yayun Zhu, Dapeng Wang, Xiaofeng Qi, Weichao Li, Zhihui Wang, Guoyong An, Nan Yu, Zuhua He, Yong-Fei Wang, Youli Xiao, Peng Zhang, and Ertao Wang. A lysm receptor heteromer mediates perception of arbuscular mycorrhizal symbiotic signal in rice. Molecular Plant, 12:1561-1576, Dec 2019. URL: https://doi.org/10.1016/j.molp.2019.10.015, doi:10.1016/j.molp.2019.10.015. This article has 207 citations and is from a highest quality peer-reviewed journal.
(he2019alysmreceptor media 7d365666): Jiangman He, Chi Zhang, Huiling Dai, Huan Liu, Xiaowei Zhang, Jun Yang, Xi Chen, Yayun Zhu, Dapeng Wang, Xiaofeng Qi, Weichao Li, Zhihui Wang, Guoyong An, Nan Yu, Zuhua He, Yong-Fei Wang, Youli Xiao, Peng Zhang, and Ertao Wang. A lysm receptor heteromer mediates perception of arbuscular mycorrhizal symbiotic signal in rice. Molecular Plant, 12:1561-1576, Dec 2019. URL: https://doi.org/10.1016/j.molp.2019.10.015, doi:10.1016/j.molp.2019.10.015. This article has 207 citations and is from a highest quality peer-reviewed journal.
(wang2024releaseofa pages 5-6): Gang Wang, Xi Chen, Chengzhi Yu, Xiaobao Shi, Wenxian Lan, Chaofeng Gao, Jun Yang, Huiling Dai, Xiaowei Zhang, Huili Zhang, Boyu Zhao, Qi Xie, Nan Yu, Zuhua He, Yu Zhang, and Ertao Wang. Release of a ubiquitin brake activates oscerk1-triggered immunity in rice. Nature, May 2024. URL: https://doi.org/10.1038/s41586-024-07418-9, doi:10.1038/s41586-024-07418-9. This article has 80 citations and is from a highest quality peer-reviewed journal.
(wang2024releaseofa pages 2-3): Gang Wang, Xi Chen, Chengzhi Yu, Xiaobao Shi, Wenxian Lan, Chaofeng Gao, Jun Yang, Huiling Dai, Xiaowei Zhang, Huili Zhang, Boyu Zhao, Qi Xie, Nan Yu, Zuhua He, Yu Zhang, and Ertao Wang. Release of a ubiquitin brake activates oscerk1-triggered immunity in rice. Nature, May 2024. URL: https://doi.org/10.1038/s41586-024-07418-9, doi:10.1038/s41586-024-07418-9. This article has 80 citations and is from a highest quality peer-reviewed journal.
(wang2024releaseofa pages 1-2): Gang Wang, Xi Chen, Chengzhi Yu, Xiaobao Shi, Wenxian Lan, Chaofeng Gao, Jun Yang, Huiling Dai, Xiaowei Zhang, Huili Zhang, Boyu Zhao, Qi Xie, Nan Yu, Zuhua He, Yu Zhang, and Ertao Wang. Release of a ubiquitin brake activates oscerk1-triggered immunity in rice. Nature, May 2024. URL: https://doi.org/10.1038/s41586-024-07418-9, doi:10.1038/s41586-024-07418-9. This article has 80 citations and is from a highest quality peer-reviewed journal.
(takagi2022chitininducedsystemicdisease pages 1-2): Momoko Takagi, Kei Hotamori, Keigo Naito, Sumire Matsukawa, Mayumi Egusa, Yoko Nishizawa, Yuri Kanno, Mitsunori Seo, Shinsuke Ifuku, Akira Mine, and Hironori Kaminaka. Chitin-induced systemic disease resistance in rice requires both oscerk1 and oscebip and is mediated via perturbation of cell-wall biogenesis in leaves. Nov 2022. URL: https://doi.org/10.3389/fpls.2022.1064628, doi:10.3389/fpls.2022.1064628. This article has 28 citations.
(takagi2022chitininducedsystemicdisease pages 2-3): Momoko Takagi, Kei Hotamori, Keigo Naito, Sumire Matsukawa, Mayumi Egusa, Yoko Nishizawa, Yuri Kanno, Mitsunori Seo, Shinsuke Ifuku, Akira Mine, and Hironori Kaminaka. Chitin-induced systemic disease resistance in rice requires both oscerk1 and oscebip and is mediated via perturbation of cell-wall biogenesis in leaves. Nov 2022. URL: https://doi.org/10.3389/fpls.2022.1064628, doi:10.3389/fpls.2022.1064628. This article has 28 citations.
(takagi2022chitininducedsystemicdisease pages 11-12): Momoko Takagi, Kei Hotamori, Keigo Naito, Sumire Matsukawa, Mayumi Egusa, Yoko Nishizawa, Yuri Kanno, Mitsunori Seo, Shinsuke Ifuku, Akira Mine, and Hironori Kaminaka. Chitin-induced systemic disease resistance in rice requires both oscerk1 and oscebip and is mediated via perturbation of cell-wall biogenesis in leaves. Nov 2022. URL: https://doi.org/10.3389/fpls.2022.1064628, doi:10.3389/fpls.2022.1064628. This article has 28 citations.
(zhang2021discriminatingsymbiosisand pages 2-3): Chi Zhang, Jiangman He, Huiling Dai, Gang Wang, Xiaowei Zhang, Chao Wang, Jincai Shi, Xi Chen, Dapeng Wang, and Ertao Wang. Discriminating symbiosis and immunity signals by receptor competition in rice. Proceedings of the National Academy of Sciences, Apr 2021. URL: https://doi.org/10.1073/pnas.2023738118, doi:10.1073/pnas.2023738118. This article has 145 citations and is from a highest quality peer-reviewed journal.
(zhang2021discriminatingsymbiosisand pages 4-5): Chi Zhang, Jiangman He, Huiling Dai, Gang Wang, Xiaowei Zhang, Chao Wang, Jincai Shi, Xi Chen, Dapeng Wang, and Ertao Wang. Discriminating symbiosis and immunity signals by receptor competition in rice. Proceedings of the National Academy of Sciences, Apr 2021. URL: https://doi.org/10.1073/pnas.2023738118, doi:10.1073/pnas.2023738118. This article has 145 citations and is from a highest quality peer-reviewed journal.
(zhang2021discriminatingsymbiosisand pages 3-4): Chi Zhang, Jiangman He, Huiling Dai, Gang Wang, Xiaowei Zhang, Chao Wang, Jincai Shi, Xi Chen, Dapeng Wang, and Ertao Wang. Discriminating symbiosis and immunity signals by receptor competition in rice. Proceedings of the National Academy of Sciences, Apr 2021. URL: https://doi.org/10.1073/pnas.2023738118, doi:10.1073/pnas.2023738118. This article has 145 citations and is from a highest quality peer-reviewed journal.
(zhang2021discriminatingsymbiosisand pages 5-6): Chi Zhang, Jiangman He, Huiling Dai, Gang Wang, Xiaowei Zhang, Chao Wang, Jincai Shi, Xi Chen, Dapeng Wang, and Ertao Wang. Discriminating symbiosis and immunity signals by receptor competition in rice. Proceedings of the National Academy of Sciences, Apr 2021. URL: https://doi.org/10.1073/pnas.2023738118, doi:10.1073/pnas.2023738118. This article has 145 citations and is from a highest quality peer-reviewed journal.
(takagi2022chitininducedsystemicdisease pages 5-6): Momoko Takagi, Kei Hotamori, Keigo Naito, Sumire Matsukawa, Mayumi Egusa, Yoko Nishizawa, Yuri Kanno, Mitsunori Seo, Shinsuke Ifuku, Akira Mine, and Hironori Kaminaka. Chitin-induced systemic disease resistance in rice requires both oscerk1 and oscebip and is mediated via perturbation of cell-wall biogenesis in leaves. Nov 2022. URL: https://doi.org/10.3389/fpls.2022.1064628, doi:10.3389/fpls.2022.1064628. This article has 28 citations.
(he2024agapin pages 2-3): Junliang He, Renliang Huang, and Xianan Xie. A gap in the recognition of two mycorrhizal factors: new insights into two lysm-type mycorrhizal receptors. Frontiers in Plant Science, Sep 2024. URL: https://doi.org/10.3389/fpls.2024.1418699, doi:10.3389/fpls.2024.1418699. This article has 6 citations.
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