Pub Date : 2026-01-05Epub Date: 2025-10-25DOI: 10.1016/j.molp.2025.10.016
Ruiqing Li, Chenfan Zheng, Binqiang Wang, Shang Dai, Yue Song, Huali Zhang, Zhiguo E, Bo Liu, Jiale Chen, Can Zhang, Haowei Fu, Ning Xu, Liangyong Ma, Qian-Hao Zhu, Vasileios Fotopoulos, Qingyao Shu, Meng Jiang
Transcriptional regulation of cold-responsive genes plays crucial roles in plant cold tolerance, but the transcription factors (TFs)-centered regulatory networks remain largely unclear. In this study, we show that Monoculm1 (MOC1), a critical TF controlling tiller number and plant height in rice, positively regulates rice cold tolerance at the seedling stage. We found that OsMPK4, a mitogen-activated protein kinase, phosphorylates and stabilizes MOC1 under cold stress. Further investigations revealed that MOC1 recruits the TFs OsbZIP79 and OsNAC5 to form a triple complex and subsequently enhances their stability by inhibiting proteasome-mediated degradation under cold stress. Notably, we found that the OsbZIP79-MOC1-OsNAC5 complex activates several cold-responsive genes, including Dehydration-responsive element-binding factor 1G (OsDREB1G), to confer rice cold tolerance. Haplotype analysis of the OsDREB1G promoter in > 10,000 rice accessions identified the favorable haplotype and key variants that endow rice cold tolerance. Collectively, our work demonstrates a pivotal role of the OsMPK4-OsbZIP79-MOC1-OsNAC5-OsDREB1G module in regulating rice cold tolerance and provides genetic targets for improving cold tolerance through molecular breeding.
{"title":"Monoculm1 confers cold tolerance at the seedling stage in rice.","authors":"Ruiqing Li, Chenfan Zheng, Binqiang Wang, Shang Dai, Yue Song, Huali Zhang, Zhiguo E, Bo Liu, Jiale Chen, Can Zhang, Haowei Fu, Ning Xu, Liangyong Ma, Qian-Hao Zhu, Vasileios Fotopoulos, Qingyao Shu, Meng Jiang","doi":"10.1016/j.molp.2025.10.016","DOIUrl":"10.1016/j.molp.2025.10.016","url":null,"abstract":"<p><p>Transcriptional regulation of cold-responsive genes plays crucial roles in plant cold tolerance, but the transcription factors (TFs)-centered regulatory networks remain largely unclear. In this study, we show that Monoculm1 (MOC1), a critical TF controlling tiller number and plant height in rice, positively regulates rice cold tolerance at the seedling stage. We found that OsMPK4, a mitogen-activated protein kinase, phosphorylates and stabilizes MOC1 under cold stress. Further investigations revealed that MOC1 recruits the TFs OsbZIP79 and OsNAC5 to form a triple complex and subsequently enhances their stability by inhibiting proteasome-mediated degradation under cold stress. Notably, we found that the OsbZIP79-MOC1-OsNAC5 complex activates several cold-responsive genes, including Dehydration-responsive element-binding factor 1G (OsDREB1G), to confer rice cold tolerance. Haplotype analysis of the OsDREB1G promoter in > 10,000 rice accessions identified the favorable haplotype and key variants that endow rice cold tolerance. Collectively, our work demonstrates a pivotal role of the OsMPK4-OsbZIP79-MOC1-OsNAC5-OsDREB1G module in regulating rice cold tolerance and provides genetic targets for improving cold tolerance through molecular breeding.</p>","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":"81-99"},"PeriodicalIF":24.1,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145372906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-03DOI: 10.1016/j.molp.2026.01.001
Chang-Xiao Tang, Shi-Jun Ma, Qi-Dong Ge, Yang Sun, Tong-Tong Liu, Man Yang, Zi-Xuan Kang, Yu-Chen Dai, Xuan Zhang, Xueman Liu, Yanyong Cao, Guan-Feng Wang
The recognition between nucleotide-binding, leucine-rich repeat (NLR) proteins and their cognate pathogen effectors often triggers the hypersensitive response (HR), a localized cell death in plants. Although NLR-interacting proteins are known to fine tune the activities of NLRs, the molecular mechanism of the kelch-containing F-box protein (FBK) in regulating NLR-mediated defense response remains unknown. Here, we report that maize ZmFBK1, but not its close homologs ZmFBK2 and ZmFBK3, modulates the homeostasis of the NLR protein Rp1-D21 and regulates Rp1-D21-mediated HR. Overexpression of ZmFBK1 suppresses the HR while mutation of ZmFBK1 enhances the HR in maize. Interestingly, ZmFBK1 is predominantly located in the autophagosome-like dots and it relocates Rp1-D21 from the nucleo-cytoplasm to the punctate dots. Moreover, we found that ZmFBK1 interacts with the autophagy-related protein ZmATG6 and facilitates autophagy-mediated degradation of Rp1-D21, thereby suppressing Rp1-D21-mediated HR. Notably, ZmFBK1 also negatively regulates the resistance to southern corn rust caused by Puccinia polysora and southern leaf blight caused by Cochliobolus heterostrophu, and both pathogens appear to promote ZmFBK1-mediated autophagy in maize. In summary, we demonstrate that ZmFBK1 and ZmATG6 suppresses Rp1-D21-mediated HR likely by sequestering Rp1-D21 in autophagosome-like structures for degradation. Our study reveals a novel mechanism about how the activity of an NLR protein is precisely regulated by an FBK protein and the autophagy pathway.
{"title":"The F-box protein ZmFBK1 facilitates autophagy-mediated degradation of maize NLR protein Rp1-D21 to suppress the hypersensitive response","authors":"Chang-Xiao Tang, Shi-Jun Ma, Qi-Dong Ge, Yang Sun, Tong-Tong Liu, Man Yang, Zi-Xuan Kang, Yu-Chen Dai, Xuan Zhang, Xueman Liu, Yanyong Cao, Guan-Feng Wang","doi":"10.1016/j.molp.2026.01.001","DOIUrl":"https://doi.org/10.1016/j.molp.2026.01.001","url":null,"abstract":"The recognition between nucleotide-binding, leucine-rich repeat (NLR) proteins and their cognate pathogen effectors often triggers the hypersensitive response (HR), a localized cell death in plants. Although NLR-interacting proteins are known to fine tune the activities of NLRs, the molecular mechanism of the kelch-containing F-box protein (FBK) in regulating NLR-mediated defense response remains unknown. Here, we report that maize ZmFBK1, but not its close homologs ZmFBK2 and ZmFBK3, modulates the homeostasis of the NLR protein Rp1-D21 and regulates Rp1-D21-mediated HR. Overexpression of ZmFBK1 suppresses the HR while mutation of ZmFBK1 enhances the HR in maize. Interestingly, ZmFBK1 is predominantly located in the autophagosome-like dots and it relocates Rp1-D21 from the nucleo-cytoplasm to the punctate dots. Moreover, we found that ZmFBK1 interacts with the autophagy-related protein ZmATG6 and facilitates autophagy-mediated degradation of Rp1-D21, thereby suppressing Rp1-D21-mediated HR. Notably, ZmFBK1 also negatively regulates the resistance to southern corn rust caused by Puccinia polysora and southern leaf blight caused by Cochliobolus heterostrophu, and both pathogens appear to promote ZmFBK1-mediated autophagy in maize. In summary, we demonstrate that ZmFBK1 and ZmATG6 suppresses Rp1-D21-mediated HR likely by sequestering Rp1-D21 in autophagosome-like structures for degradation. Our study reveals a novel mechanism about how the activity of an NLR protein is precisely regulated by an FBK protein and the autophagy pathway.","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":"53 1","pages":""},"PeriodicalIF":27.5,"publicationDate":"2026-01-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145894380","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-02DOI: 10.1016/j.molp.2025.12.030
Wei Wang, Da Chen, Huwei Sun, Surya Kant, John P. Hammond, Lei Shi, Chengcai Chu
Nitrogen (N) and phosphorus (P) are indispensable macronutrients for crop growth and productivity, whereas their excessive application in agriculture has caused severe environmental degradation. Enhancing crop N-use efficiency (NUE) and P-use efficiency (PUE) is a critical strategy to reconcile high productivity with sustainability. In this review, we systematically synthesize recent advances in the genetic basis of NUE and PUE in crops, with a focus on key traits and their associated signaling networks. We summarize the identification of N/P-efficiency genes and explore how natural variations in these genes correlate with soil nutrient availability, revealing adaptive patterns from crop domestication. Given the distinct biogeochemical behaviors of N and P, we propose tailored strategies that leverage nutrient-specific traits to optimize environment-resource coordination and yield-quality balance. Finally, we discuss strategies for developing future crops cultivars with enhanced NUE or PUE to advance sustainable agriculture.
{"title":"Genetic improvement of nitrogen- and phosphorus-use efficiency in crops: Old goals with new aspirations","authors":"Wei Wang, Da Chen, Huwei Sun, Surya Kant, John P. Hammond, Lei Shi, Chengcai Chu","doi":"10.1016/j.molp.2025.12.030","DOIUrl":"https://doi.org/10.1016/j.molp.2025.12.030","url":null,"abstract":"Nitrogen (N) and phosphorus (P) are indispensable macronutrients for crop growth and productivity, whereas their excessive application in agriculture has caused severe environmental degradation. Enhancing crop N-use efficiency (NUE) and P-use efficiency (PUE) is a critical strategy to reconcile high productivity with sustainability. In this review, we systematically synthesize recent advances in the genetic basis of NUE and PUE in crops, with a focus on key traits and their associated signaling networks. We summarize the identification of N/P-efficiency genes and explore how natural variations in these genes correlate with soil nutrient availability, revealing adaptive patterns from crop domestication. Given the distinct biogeochemical behaviors of N and P, we propose tailored strategies that leverage nutrient-specific traits to optimize environment-resource coordination and yield-quality balance. Finally, we discuss strategies for developing future crops cultivars with enhanced NUE or PUE to advance sustainable agriculture.","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":"127 1","pages":""},"PeriodicalIF":27.5,"publicationDate":"2026-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145894381","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Both activation and termination of DNA damage response (DDR) are essential to maintain genome stability. It is well-known that the histone variant H2AX is rapidly phosphorylated to activate DDR in eukaryotes. But how H2AX signaling is terminated remains poorly understood, especially in plants. Through forward genetic screening in Arabidopsis, we find that the DNA Damage Response Mutant 5 (ddrm5) mutant is hypersensitive to DNA damage-inducing reagents. Gene mapping and genetic complementation analysis reveal that DDRM5 encodes a plant-unique phosphatase MAIL3, whose phosphatase domain is necessary and sufficient for its function in DDR. Biochemically, MAIL3 physically interacts with and dephosphorylates H2AX, promoting its polyubiquitination at Lys103 and Lys127 by the E3 ubiquitin ligase SCFAFB1, which results in H2AX degradation through the proteasome. Genetically, loss of H2AX or overexpression of AFB1 rescue the DDR defects of the mail3 mutant. Taken together, this study identifies MAIL3 and SCFAFB1 as the first phosphatase and the first E3 ubiquitin ligase for plant H2AX, highlighting the importance of H2AX dephosphorylation and polyubiquitination in DDR termination.
{"title":"Dephosphorylation and polyubiquitination of the histone variant H2AX coordinately terminate DNA damage signaling in Arabidopsis.","authors":"Xuerui Lu, Xiaodan Yu, Zhiping Deng, Zhichao Wang, Lvwen Zhang, Shixi Shi, Lili Wang, Shunping Yan","doi":"10.1016/j.molp.2025.12.029","DOIUrl":"https://doi.org/10.1016/j.molp.2025.12.029","url":null,"abstract":"<p><p>Both activation and termination of DNA damage response (DDR) are essential to maintain genome stability. It is well-known that the histone variant H2AX is rapidly phosphorylated to activate DDR in eukaryotes. But how H2AX signaling is terminated remains poorly understood, especially in plants. Through forward genetic screening in Arabidopsis, we find that the DNA Damage Response Mutant 5 (ddrm5) mutant is hypersensitive to DNA damage-inducing reagents. Gene mapping and genetic complementation analysis reveal that DDRM5 encodes a plant-unique phosphatase MAIL3, whose phosphatase domain is necessary and sufficient for its function in DDR. Biochemically, MAIL3 physically interacts with and dephosphorylates H2AX, promoting its polyubiquitination at Lys103 and Lys127 by the E3 ubiquitin ligase SCF<sup>AFB1</sup>, which results in H2AX degradation through the proteasome. Genetically, loss of H2AX or overexpression of AFB1 rescue the DDR defects of the mail3 mutant. Taken together, this study identifies MAIL3 and SCF<sup>AFB1</sup> as the first phosphatase and the first E3 ubiquitin ligase for plant H2AX, highlighting the importance of H2AX dephosphorylation and polyubiquitination in DDR termination.</p>","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":""},"PeriodicalIF":24.1,"publicationDate":"2025-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145863869","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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