Pub Date : 2025-12-01Epub Date: 2025-09-09DOI: 10.1016/j.molp.2025.09.010
Francisco M Gámez-Arjona, José M Pardo, Francisco J Quintero
{"title":"How sodium gets sequestered in the vacuoles of salinized plants?","authors":"Francisco M Gámez-Arjona, José M Pardo, Francisco J Quintero","doi":"10.1016/j.molp.2025.09.010","DOIUrl":"10.1016/j.molp.2025.09.010","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":"2045-2047"},"PeriodicalIF":24.1,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145033798","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 : 2025-12-01Epub Date: 2025-10-01DOI: 10.1016/j.molp.2025.09.022
Se-Hwa Lee, Tae-Wuk Kim
{"title":"The fate of SMXLs at the crossroads of phosphorylation and ubiquitination.","authors":"Se-Hwa Lee, Tae-Wuk Kim","doi":"10.1016/j.molp.2025.09.022","DOIUrl":"10.1016/j.molp.2025.09.022","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":"2063-2065"},"PeriodicalIF":24.1,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145213179","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 : 2025-12-01Epub Date: 2025-09-05DOI: 10.1016/j.molp.2025.08.006
Bryony C I C Jacobs, Wolfgang Moeder, Julia M Davies, Keiko Yoshioka
{"title":"Phosphorylation as a switch: How plants fine-tune eATP-induced calcium signaling.","authors":"Bryony C I C Jacobs, Wolfgang Moeder, Julia M Davies, Keiko Yoshioka","doi":"10.1016/j.molp.2025.08.006","DOIUrl":"10.1016/j.molp.2025.08.006","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":"2048-2050"},"PeriodicalIF":24.1,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145008323","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 : 2025-12-01Epub Date: 2025-10-04DOI: 10.1016/j.molp.2025.10.002
Mei Yang, Hao Huang, Chao Xu, Xue Han, Guochen Qin, Le Chang, Fang Lin, Xuncheng Wang, Hang He, Xing Wang Deng
Plastoglobules, lipoprotein particles associated with thylakoid membranes, serve as critical hubs for chloroplast acclimation to environmental perturbations. However, the molecular mechanisms underlying plastoglobuli-associated signal perception and transduction remain poorly understood. Here, we identify a redox-regulated kinase complex in Arabidopsis that mediates plastoglobules' response to red light. Two plastoglobule-localized kinases, ACTIVITY OF BC1 COMPLEX KINASE 1 and 3 (ABC1K1 and ABC1K3), form a dynamic hetero-oligomeric complex essential for maintaining plastoquinone (PQ) pool homeostasis and optimizing photosynthetic efficiency. These kinases dynamically adjust their conformational states in response to PQ redox-state changes induced by environmental light conditions. Under preferential photosystem II (PSII) excitation induced by red light, reduced PQ pool initiates a signaling cascade through activation of the thylakoid oxidoreductase LUMEN THIOL OXIDOREDUCTASE 1 (LTO1). Activated LTO1 then oxidizes ABC1K1 at Cys107, triggering its oligomerization via inter-molecular disulfide-bond formation. This oligomeric state change leads to enhanced interaction between ABC1K1 and ABC1K3 oligomers, reconfiguring the kinase complex to relieve ABC1K3-mediated inhibition of PQ mobilization. Consequently, by restoring PQ-pool homeostasis, the ABC1K1-ABC1K3 complex mitigates PSII photodamage and safeguards photosynthesis, thereby enabling chloroplast adaptation to red light. Taken together, our findings reveal a redox-regulation mechanism by which plastoglobules integrate environmental cues with chloroplast homeostasis, providing new insights into plastoglobule-mediated stress acclimation.
{"title":"Redox-regulated plastoglobule ABC1K1-ABC1K3 kinase complex controls plastoquinone mobilization for chloroplast photosynthetic adaptation to red light.","authors":"Mei Yang, Hao Huang, Chao Xu, Xue Han, Guochen Qin, Le Chang, Fang Lin, Xuncheng Wang, Hang He, Xing Wang Deng","doi":"10.1016/j.molp.2025.10.002","DOIUrl":"10.1016/j.molp.2025.10.002","url":null,"abstract":"<p><p>Plastoglobules, lipoprotein particles associated with thylakoid membranes, serve as critical hubs for chloroplast acclimation to environmental perturbations. However, the molecular mechanisms underlying plastoglobuli-associated signal perception and transduction remain poorly understood. Here, we identify a redox-regulated kinase complex in Arabidopsis that mediates plastoglobules' response to red light. Two plastoglobule-localized kinases, ACTIVITY OF BC1 COMPLEX KINASE 1 and 3 (ABC1K1 and ABC1K3), form a dynamic hetero-oligomeric complex essential for maintaining plastoquinone (PQ) pool homeostasis and optimizing photosynthetic efficiency. These kinases dynamically adjust their conformational states in response to PQ redox-state changes induced by environmental light conditions. Under preferential photosystem II (PSII) excitation induced by red light, reduced PQ pool initiates a signaling cascade through activation of the thylakoid oxidoreductase LUMEN THIOL OXIDOREDUCTASE 1 (LTO1). Activated LTO1 then oxidizes ABC1K1 at Cys107, triggering its oligomerization via inter-molecular disulfide-bond formation. This oligomeric state change leads to enhanced interaction between ABC1K1 and ABC1K3 oligomers, reconfiguring the kinase complex to relieve ABC1K3-mediated inhibition of PQ mobilization. Consequently, by restoring PQ-pool homeostasis, the ABC1K1-ABC1K3 complex mitigates PSII photodamage and safeguards photosynthesis, thereby enabling chloroplast adaptation to red light. Taken together, our findings reveal a redox-regulation mechanism by which plastoglobules integrate environmental cues with chloroplast homeostasis, providing new insights into plastoglobule-mediated stress acclimation.</p>","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":"2119-2133"},"PeriodicalIF":24.1,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145233114","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 : 2025-12-01Epub Date: 2025-10-16DOI: 10.1016/j.molp.2025.10.011
Shilong Zhang, Lu Jiang, Huiru Chen, Huishan Liu, Minyu Xiong, Yuting Niu, Lingyi Xie, Lu Wang, Zhilei Mao, Tongtong Guo, Wenxiu Wang, Hong-Quan Yang
Gibberellin (GA) is a phytohormone that regulates key developmental processes in plants, including seed germination and photomorphogenesis. It is well established that GA signaling involves GA-triggered, 26S proteasome-dependent degradation of DELLA proteins. Whether DELLA proteins also undergo autophagic degradation to mediate GA signaling remains unclear. In this study, we investigated the responsiveness of Arabidopsis seedlings to GA and the dynamics of DELLA proteins under nutrient starvation in darkness. We found that GA-induced seed germination and skotomorphogenesis are impaired in autophagy mutants and that GA promotes the autophagic degradation of DELLA proteins. Biochemical and protein localization analyses revealed that GA promotes the nuclear export of DELLA proteins and ATG8, their co-localization in autophagosomes, and autophagosome formation. Further biochemical studies demonstrated that GA enhances the interaction between ATG8 and GID1, thereby promoting the association of ATG8 with DELLA proteins and their autophagic degradation. Through this mechanism, GA promotes seed germination and skotomorphogenesis under nutrient starvation in darkness, enabling seedlings to penetrate the soil rapidly, capture sunlight, and shift to autotrophic growth to overcome nutrient deficiency.
{"title":"Gibberellin triggers ATG8-dependent autophagic degradation of DELLA proteins to promote seed germination and skotomorphogenesis under nutrient starvation in Arabidopsis.","authors":"Shilong Zhang, Lu Jiang, Huiru Chen, Huishan Liu, Minyu Xiong, Yuting Niu, Lingyi Xie, Lu Wang, Zhilei Mao, Tongtong Guo, Wenxiu Wang, Hong-Quan Yang","doi":"10.1016/j.molp.2025.10.011","DOIUrl":"10.1016/j.molp.2025.10.011","url":null,"abstract":"<p><p>Gibberellin (GA) is a phytohormone that regulates key developmental processes in plants, including seed germination and photomorphogenesis. It is well established that GA signaling involves GA-triggered, 26S proteasome-dependent degradation of DELLA proteins. Whether DELLA proteins also undergo autophagic degradation to mediate GA signaling remains unclear. In this study, we investigated the responsiveness of Arabidopsis seedlings to GA and the dynamics of DELLA proteins under nutrient starvation in darkness. We found that GA-induced seed germination and skotomorphogenesis are impaired in autophagy mutants and that GA promotes the autophagic degradation of DELLA proteins. Biochemical and protein localization analyses revealed that GA promotes the nuclear export of DELLA proteins and ATG8, their co-localization in autophagosomes, and autophagosome formation. Further biochemical studies demonstrated that GA enhances the interaction between ATG8 and GID1, thereby promoting the association of ATG8 with DELLA proteins and their autophagic degradation. Through this mechanism, GA promotes seed germination and skotomorphogenesis under nutrient starvation in darkness, enabling seedlings to penetrate the soil rapidly, capture sunlight, and shift to autotrophic growth to overcome nutrient deficiency.</p>","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":"2101-2118"},"PeriodicalIF":24.1,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145313349","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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