The Plant CellPub Date : 2026-10-15DOI: 10.1093/plcell/koag315
Yang Li, Lingchao Kong, Yanshen Ren, Guotian Liu, Jochen Bogs, Alessandro Vannozzi, Yuejin Wang, Zhenchang Liang, Ling Yuan, Lijun Wang
{"title":"From stress perception to metabolite disposition: dynamic regulation of stilbene biosynthesis in plants","authors":"Yang Li, Lingchao Kong, Yanshen Ren, Guotian Liu, Jochen Bogs, Alessandro Vannozzi, Yuejin Wang, Zhenchang Liang, Ling Yuan, Lijun Wang","doi":"10.1093/plcell/koag315","DOIUrl":"https://doi.org/10.1093/plcell/koag315","url":null,"abstract":"Stilbenes are inducible plant specialized metabolites, best exemplified by resveratrol, a phytoalexin that links environmental perception, defense responses, and phenylpropanoid resource allocation. Stilbene accumulation may be controlled at three mechanistically distinct levels: signaling cascades that connect environmental and hormonal cues to kinase-dependent activation; combinatorial transcriptional control, which governs the response amplitude and specificity of stilbene synthase (STS) genes; and branch selection together with product disposition, which shapes the final metabolic output. Within this framework, MYB and WRKY proteins serve as major transcriptional nodes as activators or repressors, yet their regulatory effects depend on combinatorial interactions, phosphorylation events, competitive promoter occupancy, and metabolic context. We explicitly distinguish strongly supported mechanisms, defined by genetic perturbation, direct target validation, and metabolite quantification from emerging models built primarily on transient expression assays or co-expression correlations. This distinction avoids equating regulators supported by disparate levels of experimental evidence, identifies the most robust principles governing pathway control, and highlights experiments required to turn descriptive associations into causal mechanistic models. We further highlight conceptual insights extending beyond stilbene metabolism to inducible specialized metabolism in general, and outline research priorities for comparative genetics, cell-resolved analysis, and predictive pathway engineering.","PeriodicalId":501012,"journal":{"name":"The Plant Cell","volume":"150 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149187912","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The Plant CellPub Date : 2026-10-14DOI: 10.1093/plcell/koag314
Lin-Na Wang, Weicheng Wang, Hui-Min Zhang, Xin-Yu Lu, Zhong-Rong Yan, Tian-Yi Zhang, Yao Wang, Qiao-Ling Zhong, Ke Liao, Shan Yu, Liwen Jiang, Daoxin Xie, Shi Xiao
{"title":"The energy sensor SnRK1 promotes starvation-induced autophagosome formation by modulating ATG13a phosphorylation in Arabidopsis","authors":"Lin-Na Wang, Weicheng Wang, Hui-Min Zhang, Xin-Yu Lu, Zhong-Rong Yan, Tian-Yi Zhang, Yao Wang, Qiao-Ling Zhong, Ke Liao, Shan Yu, Liwen Jiang, Daoxin Xie, Shi Xiao","doi":"10.1093/plcell/koag314","DOIUrl":"https://doi.org/10.1093/plcell/koag314","url":null,"abstract":"In eukaryotes, autophagy is an evolutionarily conserved cellular degradation and recycling process that is tightly associated with cellular nutrient status. The energy sensor SNF1-RELATED KINASE 1 (SnRK1) is thought to sense nutrient starvation and induce autophagy, but how it regulates autophagosome formation in plant cells remains largely unknown. Here, we show that the SnRK1 α-catalytic subunit KIN10 regulates autophagosome formation in Arabidopsis (Arabidopsis thaliana) by interacting with and phosphorylating AUTOPHAGY-RELATED PROTEIN 13a (ATG13a), a key component of the ATG1a–ATG13a protein kinase complex involved in autophagy initiation. KIN10 directly phosphorylates ATG13a in vitro and in vivo, inhibiting its ubiquitination and increasing its abundance. Moreover, we identified ten serine residues in ATG13a that are important for KIN10-mediated phosphorylation. Transgenic plants accumulating a nonphosphorylatable ATG13a variant with mutations of these ten residues were less tolerant of starvation than ATG13a-overexpressing plants and displayed accelerated leaf senescence and lower autophagic flux. The KIN10-mediated phosphorylation of ATG13a did not affect ATG1a–ATG13a complex formation; instead, it facilitated ATG1a phosphorylation, thereby promoting autophagosome formation. Therefore, our findings suggest that the KIN10–ATG13a module modulates SnRK1-mediated autophagosome formation, likely representing a key step in integrating energy sensing and autophagy initiation in plant cells.","PeriodicalId":501012,"journal":{"name":"The Plant Cell","volume":"7 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-10-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149187906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Arsenic-sensing domain controls ACR3 transporter trafficking in\u0000 Marchantia polymorpha","authors":"Ignacy Bonter,Katarzyna Mizio,Alicja Dolzblasz,Paulina Tomaszewska,Kacper Zbieralski,Jacek Staszewski,Donata Wawrzycka,Anna Reymer,Wojciech Bialek,Verena Kriechbaumer,Jim Haseloff,Robert Wysocki,Ewa Maciaszczyk-Dziubinska","doi":"10.1093/plcell/koag306","DOIUrl":"https://doi.org/10.1093/plcell/koag306","url":null,"abstract":"Abstract Arsenic is a toxic, carcinogenic metalloid that threatens human health through contaminated water and food. Arsenite [As(III)] efflux mediated by ACR3 transporters is an ancient detoxification mechanism conserved across prokaryotes, fungi, algae, and non-angiosperm land plants, yet plant ACR3 proteins remain poorly characterized. Here, we show that MpACR3, the ACR3 ortholog from the model liverwort Marchantia polymorpha, contains an arsenic-responsive N-terminal domain that regulates intracellular trafficking. Under non-stress conditions, MpACR3 is detected in Golgi bodies as well as at the plasma membrane in plant cells, whereas As(III) promotes its relocalization to the plasma membrane. As(III) interacts with a cysteine-rich N-terminal region and stabilizes this domain, as shown by arsenite-biotin competition and increased protease resistance. Together with molecular dynamics simulations, which predicts As(III)-dependent changes in secondary structure and surface properties, these findings support a model in which ligand-induced remodeling of the N terminus modulates MpACR3 retention and trafficking. We further identify a di-arginine-containing LRCRF motif in which leucine and arginine residues are required for intracellular retention, whereas cysteine and phenylalanine residues are required for As(III)-induced relocalization to the plasma membrane. The broad conservation of related N-terminal domains in plant ACR3 transporters suggests that arsenic-regulated trafficking is a conserved plant adaptation to arsenic toxicity.","PeriodicalId":501012,"journal":{"name":"The Plant Cell","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2026-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149090391","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}