Molecular PlantPub Date : 2025-06-26DOI: 10.1016/j.molp.2025.06.015
Huiwen Chen, Junping Fan, Cheng Chi, Jun Zhao, Di Wu, Xiaoguang Lei, Xing Wang Deng, Daohua Jiang
{"title":"Structural basis of auxin recognition and transport in plant influx carrier AUX1","authors":"Huiwen Chen, Junping Fan, Cheng Chi, Jun Zhao, Di Wu, Xiaoguang Lei, Xing Wang Deng, Daohua Jiang","doi":"10.1016/j.molp.2025.06.015","DOIUrl":"https://doi.org/10.1016/j.molp.2025.06.015","url":null,"abstract":"Auxin regulates many aspects of plant growth and development, featuring polar auxin transport mediated by auxin efflux and influx carriers. AUX1 is the prominent auxin importer that actively takes up natural and synthetic auxins. However, the precise mechanisms by which AUX1 recognizes and transports auxin remain elusive. Here, we describe the cryo-electron microscopy structures of <ce:italic>Arabidopsis thaliana</ce:italic> AUX1 in apo and auxin-bound forms, revealing the structural basis for auxin recognition. AUX1 assumes the LeuT-like fold in an inward conformation. The auxin analogue 2,4-D is recognized by polar residues in the middle of AUX1. We identify a putative cation site in AUX1, which plays a role in stabilizing the inward-facing conformation. His249 undergoes a large conformational shift, and mutation of it completely abolished transport activity, suggesting a crucial role of His249 in AUX1 gating. Together, this study provides a structural foundation for a deeper comprehension of auxin influx by AUX1-like carriers.","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":"106 1","pages":""},"PeriodicalIF":27.5,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144515831","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}
{"title":"Targeted Protein Degradation and Protein-condensate Degradation for Plant Science and Crop Breeding.","authors":"Ruixia Niu, Ming Luo, Qing Wen, Yifan Xiong, Hua Dang, Guoyong Xu","doi":"10.1016/j.molp.2025.06.013","DOIUrl":"https://doi.org/10.1016/j.molp.2025.06.013","url":null,"abstract":"<p><p>Gene expression can be modulated at the DNA, RNA, or protein level, with targeted protein degradation (TPD) representing a well-established and effective strategy for directly manipulating protein function. TPD enables selective elimination of proteins, protein condensates or organelles by co-opting cellular degradation pathways-such as the ubiquitin-proteasome system, autophagy, or endocytosis-via induced proximity mechanisms. While TPD has had transformative impacts in biomedical research over the past two decades, its application in plant science has lagged behind. This gap stems from the sequential dominance of RNA interference and CRISPR technologies, as well as the complexity and cost of implementing chemical, macromolecular, and recombinant degrader platforms in plants. The recent development of genetically encoded chimeric protein degraders (GE-CPDs) offers a timely and promising alternative. These transgene-based systems provide a plant-adaptable, precise, tunable, and conditional means to control endogenous protein levels, opening new avenues for studying dynamic biological processes and engineering complex traits in crops. As genome engineering technologies continue to advance, GE-CPDs are poised to become a versatile and scalable platform for both basic plant biology and agricultural innovation. In this review, we highlight five key opportunities-Selective-Targeting, Co-Targeting, Organelle-Targeting, Conditional-Targeting, and Synthetic-Engineering (SCOCS)-that illustrate the emerging importance of TPD technologies, particularly GE-CPDs, in advancing plant science. We argue that the field is now well-positioned to harness the full potential of TPD for next-generation crop improvement.</p>","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":""},"PeriodicalIF":17.1,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144497530","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}
Molecular PlantPub Date : 2025-06-25DOI: 10.1016/j.molp.2025.06.014
Rachel Amir
{"title":"Methionine Metabolism and Biofortification in Maize: regulatory Networks and Genetic Strategies.","authors":"Rachel Amir","doi":"10.1016/j.molp.2025.06.014","DOIUrl":"https://doi.org/10.1016/j.molp.2025.06.014","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":""},"PeriodicalIF":17.1,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144506874","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}
{"title":"Suppression of TaHDA8-mediated lysine deacetylation of TaAREB3 acts as a drought adaptive mechanism in wheat root development","authors":"Zehui Liu, Qun Yang, Xingbei Liu, Jinpeng Li, Lei Zhang, Wei Chu, Jingchen Lin, Debiao Liu, Danyang Zhao, Xiao Peng, Chaowu Zeng, Mingming Xin, Yingyin Yao, Huiru Peng, Zhongfu Ni, Qixin Sun, Zhaorong Hu","doi":"10.1016/j.molp.2025.06.012","DOIUrl":"https://doi.org/10.1016/j.molp.2025.06.012","url":null,"abstract":"Wheat root systems undergo dynamic and adaptive changes to mitigate the adverse effects through elaborate regulatory mechanisms under drought stress. Elucidating and utilizing these mechanisms is highly important for breeding drought resistant wheat varieties. Here, we identify histone deacetylase TaHDA8, as a critical component in regulating wheat root elongation and drought resistance. Under drought stress, TaHDA8 can be finely tuned to alleviate its inhibition of root elongation, thereby adapting to water deficit. Interestingly, the reduction in TaHDA8 protein levels restores the DNA-binding ability of TaAREB3, a positive regulator of root elongation and drought resistance, which depends on the retention of acetylation at K248 and K281 residues. The restored DNA-binding ability of TaAREB3 activates the expression of <ce:italic>TaKOR1</ce:italic>, thus promoting root elongation by regulating cell proliferation in the root meristem. Further studies reveal that natural variations in the <ce:italic>TaKOR1</ce:italic> promoter determine the differences in TaAREB3 binding, and wheat germplasm with TaHDA8-TaAREB3-TaKOR1 regulatory module has been widely selected. Overall, this study reveals how lysine deacetylases regulate drought-responsive root development via non-histone deacetylation, providing genetic resources for improving root architecture and breeding drought-resistant wheat.","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":"47 1","pages":""},"PeriodicalIF":27.5,"publicationDate":"2025-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144337742","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}
Molecular PlantPub Date : 2025-06-19DOI: 10.1016/j.molp.2025.06.011
Pablo Mammi, Thomas Blein
{"title":"From non-coding to chromatin regulators: VIVIpary and the rise of lncRNAs in plant biology","authors":"Pablo Mammi, Thomas Blein","doi":"10.1016/j.molp.2025.06.011","DOIUrl":"https://doi.org/10.1016/j.molp.2025.06.011","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":"18 1","pages":""},"PeriodicalIF":27.5,"publicationDate":"2025-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144337750","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}
Molecular PlantPub Date : 2025-06-19DOI: 10.1016/j.molp.2025.06.010
Soyaab Islam, Kunwoong Park, Jing Xia, Eunju Kwon, Dong Young Kim
{"title":"Structural insights of gibberellin-mediated DELLA protein degradation","authors":"Soyaab Islam, Kunwoong Park, Jing Xia, Eunju Kwon, Dong Young Kim","doi":"10.1016/j.molp.2025.06.010","DOIUrl":"https://doi.org/10.1016/j.molp.2025.06.010","url":null,"abstract":"Gibberellin promotes plant growth by downregulating DELLA proteins, which act as growth repressors. In the presence of gibberellin, the gibberellin receptor GID1 binds to DELLA proteins, triggering their degradation through polyubiquitination by the SCF<ce:sup loc=\"post\">SLY1/GID2</ce:sup> ubiquitin E3 ligase. Despite extensive studies, the molecular mechanisms by which DELLA proteins assemble with SCF<ce:sup loc=\"post\">SLY1/GID2</ce:sup> to regulate plant growth remain poorly understood. Here, we present two cryo-electron microscopy structures of the <ce:italic>Arabidopsis thaliana</ce:italic> DELLA protein RGA in complex with GID1A and GID1A-SLY1-ASK2, respectively. Structural analyses revealed that RGA interacts with GID1A and SLY1 through nonoverlapping binding surfaces, stabilizing the proteins. This suggests that the SCF<ce:sup loc=\"post\">SLY1</ce:sup>-RGA-GID1A complex assembles through a stepwise stabilization process induced by gibberellin. Furthermore, structural comparison with GRAS proteins indicates that RGA does not interact with IDD family transcription factors when bound to SLY1, suggesting that DELLA protein binding to GID1/SLY1 and to transcription factors is mutually exclusive. These findings provide insights into the gibberellin-mediated regulation of transcription factor activity by DELLA proteins.","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":"25 1","pages":""},"PeriodicalIF":27.5,"publicationDate":"2025-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144337741","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}
{"title":"The transcription factor MYB44 suppresses starch synthesis to negatively regulate grain weight and yield in wheat and rice.","authors":"Yunchuan Liu, Mingming Wang, Yaojia Wang, Haixia Liu, Wei Xi, David Seung, Xiaolu Wang, Lei Zhuang, Huifang Li, Tian Li, Hongxia Liu, Jian Hou, Xu Liu, Chenyang Hao, Xueyong Zhang","doi":"10.1016/j.molp.2025.06.007","DOIUrl":"https://doi.org/10.1016/j.molp.2025.06.007","url":null,"abstract":"<p><p>Starch is the principal storage compound in wheat grain, essential for flour quality and grain weight. In this study, we identified TaMYB44, an R2R3-MYB transcription factor gene, through a genome-wide association study. The TaMYB44 homoeologs exhibited predominant expression in developing grains, with peak levels observed at 10 days after pollination. Functional analyses revealed that TaMYB44 acts as a negative regulator of starch synthesis in the endosperm and limits grain size by repressing starch synthesis-related genes and modulating secondary metabolism. Knockout mutants of TaMYB44 exhibited significantly increased starch accumulation, larger grain size, and enhanced yield stability across different growing environments. Additionally, we discovered that TaWDR1 interacts with TaMYB44, alleviating its repressive effects to restore starch synthesis and enhance grain weight. Moreover, we found that the functions of MYB44 are partially conserved in both wheat and rice, underscoring its potential as a target for genetic improvement. Our findings provide valuable insights into the transcriptional regulation of starch synthesis and present genetic resources for improving grain yield in wheat and rice.</p>","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":""},"PeriodicalIF":17.1,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144326295","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}
Molecular PlantPub Date : 2025-06-18DOI: 10.1016/j.molp.2025.06.008
Vincent E Cerbantez-Bueno, G Venugopala Reddy
{"title":"Temperature regulation of CLAVATA3 Arabinosylation.","authors":"Vincent E Cerbantez-Bueno, G Venugopala Reddy","doi":"10.1016/j.molp.2025.06.008","DOIUrl":"10.1016/j.molp.2025.06.008","url":null,"abstract":"","PeriodicalId":19012,"journal":{"name":"Molecular Plant","volume":" ","pages":""},"PeriodicalIF":17.1,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144333540","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}