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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase OsCCaMK (also called OsDMI3; rice gene CCAMK) is a Ca2+/calmodulin (CaM)-regulated kinase that decodes intracellular/nuclear calcium signatures and couples them to transcriptional programs and stress signaling outputs. In rice, OsCCaMK is an essential core component of the common symbiosis signaling pathway (CSSP) required for arbuscular mycorrhizal (AM) colonization, acting upstream of the transcription factor CYCLOPS/IPD3. Beyond symbiosis, OsDMI3 regulates abiotic-stress tolerance, including saline-alkaline tolerance via ion-homeostasis outputs, and has been positioned (via 2023 primary work cited by 2024 reviews) as a kinase that phosphorylates OsRBOHB, promoting H2O2 production to potentiate ABA signaling and drought-related responses. (ni2020calciumcalmodulindependentproteinkinase pages 3-4, gutjahr2008arbuscularmycorrhiza–specificsignaling pages 1-2, wang2024reactiveoxygenspecies pages 20-21)
The target described by UniProt accession Q6AVM3 (rice Oryza sativa ssp. japonica) matches the rice CCaMK literature in which CCAMK is explicitly identified as Os05g41090 (CCAMK) and described as a calcium/calmodulin-dependent protein kinase containing a CaM-binding region and EF-hands. In Gutjahr et al. (2008), the gene is listed as “Os05g41090 (CCAMK)”, and a Tos17 insertion allele is described as being between the calmodulin-binding domain and the three EF-hands, consistent with the UniProt domain architecture (kinase + CaM-binding/autoinhibitory region + EF-hands). (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 13-14)
Independent rice stress literature uses the name OsDMI3 for this CCaMK: Ni et al. (2020) repeatedly refers to “a rice Ca2+/calmodulin-dependent protein kinase, OsDMI3”, i.e., OsDMI3 = rice CCaMK. (ni2020calciumcalmodulindependentproteinkinase pages 1-3)
Operational definitions used in this report
- CCaMK (calcium- and calmodulin-dependent protein kinase): a plant Ser/Thr kinase regulated by Ca2+ binding and Ca2+/CaM, often functioning as a decoder of calcium oscillations/spiking in symbiotic and stress signaling. (wu2023receptorkinasesand pages 9-11)
- CSSP/CSP/SYM pathway: a conserved signaling pathway for intracellular symbioses (AM and, in legumes, nodulation) that transduces symbiont perception into nuclear Ca2+ spiking and transcriptional reprogramming. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 1-2, wu2023receptorkinasesand pages 9-11)
OsDMI3/OsCCaMK is experimentally shown to have protein kinase activity in rice roots using an in-gel kinase assay. In Ni et al. (2020), OsDMI3 was immunoprecipitated and assayed using myelin basic protein (MBP) as an in vitro substrate, confirming enzymatic activity consistent with a Ser/Thr protein kinase. (ni2020calciumcalmodulindependentproteinkinase pages 3-4)
Assay conditions supporting Ca2+/CaM regulation: The kinase reaction mixture included 0.5 mM CaCl2 and 2 mM calmodulin, along with Mg2+ (5 mM MgCl2), indicating activity was evaluated under Ca2+/CaM-activating conditions and supporting classification as Ca2+/CaM-dependent in biochemical assays. (ni2020calciumcalmodulindependentproteinkinase pages 3-4)
Best-supported direct downstream target in symbiosis signaling: Rice symbiosis work places CCAMK immediately upstream of CYCLOPS/IPD3 and states that CYCLOPS interacts with CCAMK and is a phosphorylation substrate of CCAMK, making CYCLOPS the most directly supported signaling substrate relevant to functional annotation. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 2-3)
ABA/ROS axis target (from 2023 primary study as summarized in 2024 sources): A 2024 authoritative review in Journal of Integrative Plant Biology explicitly states that the CaM-dependent kinase OsDMI3 “was recently shown to phosphorylate OsRBOHB and promote H2O2 production to potentiate ABA signaling and drought stress tolerance in rice (Wang et al., 2023).” (wang2024reactiveoxygenspecies pages 20-21)
In addition, a 2024 rice RBOH genetics paper quotes the title-level conclusion of the 2023 Mol Plant study: “Phosphorylation of OsRbohB by the protein kinase OsDMI3 promotes H2O2 production to potentiate ABA responses in rice.” (zhu2024identificationofnadph pages 14-15)
Important limitation: the 2023 primary paper itself was not retrievable in this run, so the exact phosphosites/kinetics cannot be directly extracted here; the statement is nevertheless attributable to authoritative 2024 secondary sources that cite the primary work. (zhu2024identificationofnadph pages 14-15, wang2024reactiveoxygenspecies pages 20-21)
A current mechanistic synthesis of CCaMK regulation in the CSSP describes activation as requiring Ca2+ binding to EF-hands, CaM binding, and autophosphorylation at a conserved threonine. The 2023 CSSP chapter states that CCaMK activation requires Ca2+ binding to three EF-hands, CaM binding, and autophosphorylation at Thr265. (wu2023receptorkinasesand pages 9-11)
Consistent with rice CCAMK structural features, the rice AM genetics paper notes a CCAMK insertion allele occurring between the CaM-binding domain and the three EF hands, supporting the same architecture for rice CCAMK. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 13-14)
Mechanistic work summarized in authoritative dissertations (largely in the Lotus japonicus CCaMK system but describing conserved residues and logic) supports the following regulatory principles:
- CCaMK is regulated by Ca2+ and Ca2+/CaM and possesses a CaM-binding/autoinhibitory domain; autophosphorylation at a conserved threonine (T265 in canonical numbering) stabilizes an autoinhibitory conformation and phosphomimetic substitutions can generate autoactive variants. (katzer2017structurefunctionand pages 27-30, bellon2021phosphorylationofthe pages 43-46)
- A conserved phosphorylation site in the CaM-binding region (S337 in Lotus) is described as a negative regulator; phosphomimetic variants reduce CaM binding and substrate phosphorylation. (bellon2021phosphorylationofthe pages 43-46, singh2014thecalciumsignature pages 64-68)
These mechanistic points are relevant for rice functional annotation because the rice protein has matching domains (UniProt Q6AVM3) and rice genetic lesions map to the CaM/EF-hand junction. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 13-14)
Direct rice subcellular localization experiments were not retrieved in the available rice texts in this run; however, CCaMK is consistently framed as a nuclear calcium-spiking decoder in CSSP models, acting with the transcription factor CYCLOPS. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 1-2, wu2023receptorkinasesand pages 9-11)
Supporting experimental evidence from a closely related plant system indicates CCaMK localization to the root cell nucleus, consistent with the nuclear Ca2+ decoding role and interaction with CYCLOPS. This supports a conservative localization inference for OsCCaMK as acting primarily in the nucleus in symbiosis signaling, while acknowledging that direct rice localization should be confirmed experimentally. (shimoda2019kinaseactivitydependentstability pages 1-2)
In rice AM symbiosis genetics, CCAMK/DMI3 is described as acting downstream of Ca2+ spiking in the SYM pathway and is thought to transduce/decipher calcium signals; CCAMK interacts with and phosphorylates CYCLOPS/IPD3. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 1-2, gutjahr2008arbuscularmycorrhiza–specificsignaling pages 2-3)
Phenotypic evidence in rice: Rice ccamk mutants show impaired AM interactions and failure to establish normal colonization patterns; the extracted figure panels from Gutjahr et al. include a pathway schematic and quantitative colonization readouts showing reduced colonization for ccamk-1 and ccamk-2, plus microscopy panels consistent with entry/penetration defects and failure of cortical progression. (gutjahr2008arbuscularmycorrhiza–specificsignaling media ba832510, gutjahr2008arbuscularmycorrhiza–specificsignaling media 5b9ed253, gutjahr2008arbuscularmycorrhiza–specificsignaling media 6cac6fba)
Current expert model (2023): A conserved downstream module in CSSP is described as CCaMK–CYCLOPS–DELLA, where CCaMK phosphorylates CYCLOPS and DELLA proteins help route signaling outputs toward symbiosis-specific transcriptional programs such as RAM1 (AM) or NIN (nodulation in legumes). (wu2023receptorkinasesand pages 3-7, wu2023receptorkinasesand pages 1-3)
A 2024 bioRxiv preprint synthesizes and extends evidence that the SYMRK–CCaMK–CYCLOPS module is deeply conserved: it argues that CCaMK is essential for AM symbiosis in legumes and monocots including rice and barley, and then demonstrates essentiality of the orthologous module in the liverwort Marchantia paleacea, supporting conservation across ~450 million years. (vernie2024conservationofsymbiotic pages 3-6)
Ni et al. (2020) provides direct rice evidence that OsDMI3 positively regulates saline-alkaline tolerance in roots. Key observations:
- Treatment: 75 mM NaHCO3 (pH 8.0) induces OsDMI3 transcript levels and kinase activity; activity increase is observed 1 h after treatment in the in-gel kinase assay. (ni2020calciumcalmodulindependentproteinkinase pages 3-4)
- Physiological outputs: OsDMI3 overexpression lines show greater root length and fresh weight under stress and reduced Na+ accumulation and reduced Na+ and H+ influx (root meristem zone) relative to wild type; knockouts show the opposite trend. (ni2020calciumcalmodulindependentproteinkinase pages 4-6, ni2020calciumcalmodulindependentproteinkinase pages 3-4)
- Transcriptional outputs: OsDMI3 upregulates OsSOS1 and PM H+-ATPase genes OsA3 and OsA8 under saline-alkaline stress. (ni2020calciumcalmodulindependentproteinkinase pages 4-6)
Direct vs indirect effects: The study explicitly notes that whether OsDMI3 directly phosphorylates the transport machinery remains unresolved; therefore, OsSOS1 and PM H+-ATPase genes should currently be treated as downstream outputs rather than confirmed direct substrates. (ni2020calciumcalmodulindependentproteinkinase pages 4-6)
A 2024 high-impact review explicitly integrates OsDMI3 into a ROS/ABA regulatory circuit in rice: OsDMI3 phosphorylates OsRBOHB (NADPH oxidase) to promote H2O2 production, potentiating ABA signaling and drought stress tolerance. (wang2024reactiveoxygenspecies pages 20-21)
This mechanism provides a concrete biochemical bridge from Ca2+/CaM-dependent kinase activity to ROS production, consistent with broader expert frameworks that RBOH activity must be tightly regulated in drought responses (e.g., stomatal closure). (wang2024reactiveoxygenspecies pages 20-21)
Ni et al. (2020) makes explicit translational claims: the authors conclude that OsDMI3 is “an important genetic target” for protecting rice growth under saline-alkaline stress and “a promising candidate gene for breeding saline-alkaline tolerant rice varieties.” (ni2020calciumcalmodulindependentproteinkinase pages 1-3, ni2020calciumcalmodulindependentproteinkinase pages 4-6)
The 2023 CSSP chapter emphasizes cross-species functional conservation, stating that rice OsDMI3 can functionally complement AM symbiosis in Medicago truncatula (and only partially restore nodulation), supporting the concept that conserved CCaMK modules can be transplanted or tuned across species. (wu2023receptorkinasesand pages 9-11)
Limitations on real-world deployment: The retrieved sources do not describe commercial cultivars or field-deployed OsDMI3-edited/overexpression lines; the applications are primarily at the proof-of-concept gene-target and pathway-conservation stage in the available texts. (ni2020calciumcalmodulindependentproteinkinase pages 4-6, wu2023receptorkinasesand pages 9-11)
The following table consolidates the major functional-annotation facts, with URLs and dates.
| Aspect | Key finding for rice OsCCaMK/OsDMI3 (Q6AVM3) | Evidence / quantitative detail | Source (date, URL) |
|---|---|---|---|
| Target identity / disambiguation | The literature consistently identifies rice CCAMK/CCaMK as OsDMI3, a calcium/calmodulin-dependent protein kinase in Oryza sativa; a classic rice locus used in foundational AM papers is Os05g41090 (CCAMK). A Tos17 insertion was reported between the CaM-binding domain and three EF hands, matching the UniProt domain architecture. | Explicit rice identifier Os05g41090 (CCAMK); mutant structure supports kinase + CaM-binding + EF-hand identity. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 13-14, ni2020calciumcalmodulindependentproteinkinase pages 1-3) | Gutjahr et al., Plant Cell (2008), https://doi.org/10.1105/tpc.108.062414; Ni et al., Plant Signaling & Behavior (2020), https://doi.org/10.1080/15592324.2020.1813999 |
| Molecular function / enzyme class | OsCCaMK/OsDMI3 is a Ser/Thr protein kinase that acts as a Ca2+/calmodulin-responsive decoder of calcium signals. | In rice, kinase activity was measured by in-gel kinase assay after immunoprecipitation; assay used myelin basic protein (MBP) as substrate. Activity increased after saline-alkaline treatment. (ni2020calciumcalmodulindependentproteinkinase pages 1-3, ni2020calciumcalmodulindependentproteinkinase pages 3-4) | Ni et al. (2020), https://doi.org/10.1080/15592324.2020.1813999 |
| Assay conditions for kinase activity | Rice OsDMI3 kinase assays were performed under Ca2+/CaM-containing conditions, supporting biochemical classification as a Ca2+/CaM-dependent kinase. | Reaction conditions included 25 mM Tris-HCl pH 7.5, 5 mM MgCl2, 0.5 mM CaCl2, 2 mM calmodulin; kinase activity significantly increased 1 h after 75 mM NaHCO3 (pH 8.0) treatment. (ni2020calciumcalmodulindependentproteinkinase pages 3-4) | Ni et al. (2020), https://doi.org/10.1080/15592324.2020.1813999 |
| Known substrate / interacting partner | The best-supported direct downstream target for plant CCaMKs, including the rice symbiosis framework, is CYCLOPS/IPD3, which interacts with and is phosphorylated by CCaMK. | Rice symbiosis literature states CYCLOPS is a phosphorylation substrate of CCAMK; pathway models place CCAMK → CYCLOPS downstream of Ca2+ spiking. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 1-2, gutjahr2008arbuscularmycorrhiza–specificsignaling pages 2-3, gutjahr2008arbuscularmycorrhiza–specificsignaling media ba832510) | Gutjahr et al. (2008), https://doi.org/10.1105/tpc.108.062414 |
| Putative downstream effectors in saline-alkaline stress | Under saline-alkaline stress, OsDMI3 promotes expression of OsSOS1 and plasma-membrane H+-ATPase genes OsA3 and OsA8; these are supported as downstream outputs, but direct phosphorylation was not established in this paper. | After 75 mM NaHCO3, OsDMI3 OE lines showed lower root Na+ accumulation and lower Na+ / H+ influx than WT; KO lines showed the opposite. The study explicitly notes that direct phosphorylation of these transport systems remains unresolved. (ni2020calciumcalmodulindependentproteinkinase pages 4-6, ni2020calciumcalmodulindependentproteinkinase pages 3-4) | Ni et al. (2020), https://doi.org/10.1080/15592324.2020.1813999 |
| Regulation by Ca2+, CaM, autoinhibition | CCaMK family proteins are regulated by both Ca2+ and Ca2+/CaM and contain a CaM-binding/autoinhibitory domain. Conserved regulatory phosphorylation sites include T265 (autophosphorylation-associated autoinhibitory control) and S337 (within/near the CaM-binding region; negative regulatory role). | Family-level mechanistic work shows T265D can create autoactive forms; S337D reduces CaM binding/substrate phosphorylation; these data are strong for plant CCaMKs, though not all were measured directly for rice OsDMI3 in the retrieved rice papers. (katzer2017structurefunctionand pages 27-30, bellon2021phosphorylationofthe pages 43-46, singh2014thecalciumsignature pages 64-68) | Katzer dissertation (2017), https://doi.org/10.5282/edoc.24793; Bellon dissertation (2021), https://doi.org/10.5282/edoc.28624; Singh dissertation (2014), https://doi.org/10.5282/edoc.16950 |
| Domain architecture / substrate-sensing logic | Plant CCaMKs possess an N-terminal kinase domain, a CaM-binding/autoinhibitory region, and a C-terminal EF-hand Ca2+-binding region; these features underpin calcium-signal decoding. | Retrieved texts describe two visinin-like plus one non-canonical EF-hand organization and show that disruption/deletion of EF-hand region impairs symbiotic function. Rice mutant insertion between CaM-binding region and EF hands further supports this architecture. (katzer2017structurefunctionand pages 27-30, gutjahr2008arbuscularmycorrhiza–specificsignaling pages 13-14, singh2014thecalciumsignature pages 64-68) | Katzer (2017), https://doi.org/10.5282/edoc.24793; Gutjahr et al. (2008), https://doi.org/10.1105/tpc.108.062414; Singh (2014), https://doi.org/10.5282/edoc.16950 |
| Subcellular localization | CCaMK is most strongly supported as a nuclear signaling kinase in symbiosis, where it forms a complex with CYCLOPS and decodes nuclear Ca2+ spiking. | Nuclear localization is directly supported in Lotus and used in cross-species mechanistic interpretation; rice pathway papers place CCAMK downstream of nuclear Ca2+ spiking and upstream of CYCLOPS, consistent with nuclear action. Direct rice localization evidence was not retrieved here. (katzer2017structurefunctionand pages 27-30, shimoda2019kinaseactivitydependentstability pages 1-2, gutjahr2008arbuscularmycorrhiza–specificsignaling pages 1-2) | Katzer (2017), https://doi.org/10.5282/edoc.24793; Shimoda et al., Planta (2019), https://doi.org/10.1007/s00425-019-03264-6; Gutjahr et al. (2008), https://doi.org/10.1105/tpc.108.062414 |
| Core pathway role | OsCCaMK/OsDMI3 is a central component of the common symbiosis signaling pathway (CSSP/SYM pathway), acting downstream of Ca2+ spiking and upstream of transcriptional reprogramming via CYCLOPS. | Rice ccamk mutants display impaired AM interactions and altered AM-marker gene expression; pathway figures explicitly place CASTOR/POLLUX → Ca2+ spiking → CCAMK → CYCLOPS. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 1-2, gutjahr2008arbuscularmycorrhiza–specificsignaling media ba832510) | Gutjahr et al. (2008), https://doi.org/10.1105/tpc.108.062414 |
| AM symbiosis phenotype in rice | Loss of rice CCAMK strongly impairs arbuscular mycorrhizal colonization, with fungal entry defects and failure of proper cortical colonization. | Figure evidence from the rice AM study shows reduced root-length colonization in ccamk-1 and ccamk-2 and abnormal epidermal/rhizodermal fungal structures without normal cortical progression. (gutjahr2008arbuscularmycorrhiza–specificsignaling media ba832510, gutjahr2008arbuscularmycorrhiza–specificsignaling media 5b9ed253, gutjahr2008arbuscularmycorrhiza–specificsignaling media 6cac6fba) | Gutjahr et al. (2008), https://doi.org/10.1105/tpc.108.062414 |
| Saline-alkaline tolerance role | Beyond symbiosis, OsDMI3 positively regulates saline-alkaline tolerance in rice roots by modulating ion homeostasis. | Experimental setup: 3-day-old seedlings treated with 75 mM NaHCO3; Na+/H+ fluxes measured after 24 h by NMT; RT-PCR after 6 h; flux data were means ± SEM of 6 independent experiments. OE plants had longer roots/higher fresh weight under stress; KO plants were more sensitive. (ni2020calciumcalmodulindependentproteinkinase pages 4-6, ni2020calciumcalmodulindependentproteinkinase pages 3-4) | Ni et al. (2020), https://doi.org/10.1080/15592324.2020.1813999 |
| Recent / current understanding | Recent reviews and comparative studies continue to treat CCaMK as an ancient, highly conserved symbiotic signaling hub, with the CCaMK–CYCLOPS module retained across land-plant evolution. | 2023 review summarizes CCaMK-CYCLOPS-DELLA as central to AM signaling; 2024 evolutionary study argues conservation of the module across ~450 million years of land-plant evolution. These are not rice-specific functional assays but support current expert consensus. (gutjahr2008arbuscularmycorrhiza–specificsignaling pages 1-2) | Wu et al., IntechOpen chapter (2023), https://doi.org/10.5772/intechopen.107261; Vernié et al., bioRxiv (2024), https://doi.org/10.1101/2024.01.16.575147 |
Table: This table summarizes experimentally supported and strongly inferred functional-annotation facts for rice OsCCaMK/OsDMI3, including identity verification, kinase activity, regulation, localization, pathway role, and key quantitative details with source URLs.
The following extracted figure panels from Gutjahr et al. (2008) support (i) CCAMK’s placement in the rice SYM/CSSP pathway and (ii) AM colonization phenotypes of ccamk mutants.
References
(ni2020calciumcalmodulindependentproteinkinase pages 3-4): Lan Ni, Shuang Wang, Tao Shen, Qingwen Wang, Chao Chen, Jixing Xia, and Mingyi Jiang. Calcium/calmodulin-dependent protein kinase osdmi3 positively regulates saline-alkaline tolerance in rice roots. Plant Signaling & Behavior, Aug 2020. URL: https://doi.org/10.1080/15592324.2020.1813999, doi:10.1080/15592324.2020.1813999. This article has 32 citations and is from a peer-reviewed journal.
(gutjahr2008arbuscularmycorrhiza–specificsignaling pages 1-2): Caroline Gutjahr, Mari Banba, Vincent Croset, Kyungsook An, Akio Miyao, Gynheung An, Hirohiko Hirochika, Haruko Imaizumi-Anraku, and Uta Paszkowski. Arbuscular mycorrhiza–specific signaling in rice transcends the common symbiosis signaling pathway[w]. The Plant Cell Online, 20:2989-3005, Nov 2008. URL: https://doi.org/10.1105/tpc.108.062414, doi:10.1105/tpc.108.062414. This article has 338 citations.
(wang2024reactiveoxygenspecies pages 20-21): Pengtao Wang, Wen‐Cheng Liu, Chao Han, Situ Wang, Ming‐Yi Bai, and Chun‐Peng Song. Reactive oxygen species: multidimensional regulators of plant adaptation to abiotic stress and development. Journal of Integrative Plant Biology, 66:330-367, Jan 2024. URL: https://doi.org/10.1111/jipb.13601, doi:10.1111/jipb.13601. This article has 487 citations and is from a peer-reviewed journal.
(gutjahr2008arbuscularmycorrhiza–specificsignaling pages 13-14): Caroline Gutjahr, Mari Banba, Vincent Croset, Kyungsook An, Akio Miyao, Gynheung An, Hirohiko Hirochika, Haruko Imaizumi-Anraku, and Uta Paszkowski. Arbuscular mycorrhiza–specific signaling in rice transcends the common symbiosis signaling pathway[w]. The Plant Cell Online, 20:2989-3005, Nov 2008. URL: https://doi.org/10.1105/tpc.108.062414, doi:10.1105/tpc.108.062414. This article has 338 citations.
(ni2020calciumcalmodulindependentproteinkinase pages 1-3): Lan Ni, Shuang Wang, Tao Shen, Qingwen Wang, Chao Chen, Jixing Xia, and Mingyi Jiang. Calcium/calmodulin-dependent protein kinase osdmi3 positively regulates saline-alkaline tolerance in rice roots. Plant Signaling & Behavior, Aug 2020. URL: https://doi.org/10.1080/15592324.2020.1813999, doi:10.1080/15592324.2020.1813999. This article has 32 citations and is from a peer-reviewed journal.
(wu2023receptorkinasesand pages 9-11): Jiashan Wu, Weiyun Wang, Hui Zhu, and Yangrong Cao. Receptor kinases and signal pathway in the arbuscular mycorrhizal symbiosis. Arbuscular Mycorrhizal Fungi in Agriculture - New Insights, Mar 2023. URL: https://doi.org/10.5772/intechopen.107261, doi:10.5772/intechopen.107261. This article has 5 citations.
(gutjahr2008arbuscularmycorrhiza–specificsignaling pages 2-3): Caroline Gutjahr, Mari Banba, Vincent Croset, Kyungsook An, Akio Miyao, Gynheung An, Hirohiko Hirochika, Haruko Imaizumi-Anraku, and Uta Paszkowski. Arbuscular mycorrhiza–specific signaling in rice transcends the common symbiosis signaling pathway[w]. The Plant Cell Online, 20:2989-3005, Nov 2008. URL: https://doi.org/10.1105/tpc.108.062414, doi:10.1105/tpc.108.062414. This article has 338 citations.
(zhu2024identificationofnadph pages 14-15): Yong-Xing Zhu, Hao Su, Xin-Xian Liu, Ji-Fen Sun, Ling Xiang, Yan-Jing Liu, Zhang-Wei Hu, Xiao-Yu Xiong, Xue-mei Yang, Sadam Hussain Bhutto, Guobang Li, Yuanying Peng, He Wang, Xu Shen, Zhi-Xue Zhao, Ji-Wei Zhang, Yan-Yan Huang, Jing Fan, Wen-ming Wang, and Yan Li. Identification of nadph oxidase genes crucial for rice multiple disease resistance and yield traits. Rice, Jan 2024. URL: https://doi.org/10.1186/s12284-023-00678-5, doi:10.1186/s12284-023-00678-5. This article has 22 citations and is from a peer-reviewed journal.
(katzer2017structurefunctionand pages 27-30): Katja Katzer. Structure, function and regulation of the ccamk/cyclops complex during root symbioses. Dissertation, Jan 2017. URL: https://doi.org/10.5282/edoc.24793, doi:10.5282/edoc.24793. This article has 0 citations.
(bellon2021phosphorylationofthe pages 43-46): Phosphorylation of the transcription factor Cyclops from L. japonicus modulates its activity and its interaction with CCaMK This article has 0 citations.
(singh2014thecalciumsignature pages 64-68): Sylvia Singh. The calcium signature decoding ccamk/cyclops complex activates the transcription of symbiosis associated genes. Dissertation, Jan 2014. URL: https://doi.org/10.5282/edoc.16950, doi:10.5282/edoc.16950. This article has 1 citations.
(shimoda2019kinaseactivitydependentstability pages 1-2): Yoshikazu Shimoda, Haruko Imaizumi-Anraku, and Makoto Hayashi. Kinase activity-dependent stability of calcium/calmodulin-dependent protein kinase of lotus japonicus. Planta, 250:1773-1779, Aug 2019. URL: https://doi.org/10.1007/s00425-019-03264-6, doi:10.1007/s00425-019-03264-6. This article has 5 citations and is from a peer-reviewed journal.
(gutjahr2008arbuscularmycorrhiza–specificsignaling media ba832510): Caroline Gutjahr, Mari Banba, Vincent Croset, Kyungsook An, Akio Miyao, Gynheung An, Hirohiko Hirochika, Haruko Imaizumi-Anraku, and Uta Paszkowski. Arbuscular mycorrhiza–specific signaling in rice transcends the common symbiosis signaling pathway[w]. The Plant Cell Online, 20:2989-3005, Nov 2008. URL: https://doi.org/10.1105/tpc.108.062414, doi:10.1105/tpc.108.062414. This article has 338 citations.
(gutjahr2008arbuscularmycorrhiza–specificsignaling media 5b9ed253): Caroline Gutjahr, Mari Banba, Vincent Croset, Kyungsook An, Akio Miyao, Gynheung An, Hirohiko Hirochika, Haruko Imaizumi-Anraku, and Uta Paszkowski. Arbuscular mycorrhiza–specific signaling in rice transcends the common symbiosis signaling pathway[w]. The Plant Cell Online, 20:2989-3005, Nov 2008. URL: https://doi.org/10.1105/tpc.108.062414, doi:10.1105/tpc.108.062414. This article has 338 citations.
(gutjahr2008arbuscularmycorrhiza–specificsignaling media 6cac6fba): Caroline Gutjahr, Mari Banba, Vincent Croset, Kyungsook An, Akio Miyao, Gynheung An, Hirohiko Hirochika, Haruko Imaizumi-Anraku, and Uta Paszkowski. Arbuscular mycorrhiza–specific signaling in rice transcends the common symbiosis signaling pathway[w]. The Plant Cell Online, 20:2989-3005, Nov 2008. URL: https://doi.org/10.1105/tpc.108.062414, doi:10.1105/tpc.108.062414. This article has 338 citations.
(wu2023receptorkinasesand pages 3-7): Jiashan Wu, Weiyun Wang, Hui Zhu, and Yangrong Cao. Receptor kinases and signal pathway in the arbuscular mycorrhizal symbiosis. Arbuscular Mycorrhizal Fungi in Agriculture - New Insights, Mar 2023. URL: https://doi.org/10.5772/intechopen.107261, doi:10.5772/intechopen.107261. This article has 5 citations.
(wu2023receptorkinasesand pages 1-3): Jiashan Wu, Weiyun Wang, Hui Zhu, and Yangrong Cao. Receptor kinases and signal pathway in the arbuscular mycorrhizal symbiosis. Arbuscular Mycorrhizal Fungi in Agriculture - New Insights, Mar 2023. URL: https://doi.org/10.5772/intechopen.107261, doi:10.5772/intechopen.107261. This article has 5 citations.
(vernie2024conservationofsymbiotic pages 3-6): Tatiana Vernié, Mélanie Rich, Tifenn Pellen, Eve Teyssier, Vincent Garrigues, Lucie Chauderon, Lauréna Medioni, Fabian van Beveren, Cyril Libourel, Jean Keller, Camille Girou, Corinne Lefort, Aurélie Le Ru, Didier Reinhardt, Kyoichi Kodama, Syota Shimazaki, Patrice Morel, Junko Kyozuka, Malick Mbengue, Michiel Vandenbussche, and Pierre-Marc Delaux. Conservation of symbiotic signalling across 450 million years of plant evolution. bioRxiv, Jan 2024. URL: https://doi.org/10.1101/2024.01.16.575147, doi:10.1101/2024.01.16.575147. This article has 5 citations.
(ni2020calciumcalmodulindependentproteinkinase pages 4-6): Lan Ni, Shuang Wang, Tao Shen, Qingwen Wang, Chao Chen, Jixing Xia, and Mingyi Jiang. Calcium/calmodulin-dependent protein kinase osdmi3 positively regulates saline-alkaline tolerance in rice roots. Plant Signaling & Behavior, Aug 2020. URL: https://doi.org/10.1080/15592324.2020.1813999, doi:10.1080/15592324.2020.1813999. This article has 32 citations and is from a peer-reviewed journal.