{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,9]],"date-time":"2026-08-09T04:41:54Z","timestamp":1786250514257,"version":"build-2736575974"},"reference-count":36,"publisher":"MDPI AG","issue":"16","license":[{"start":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T00:00:00Z","timestamp":1786060800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"Natural Science Foundation of China","doi-asserted-by":"crossref","award":["32470299"],"award-info":[{"award-number":["32470299"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Jiangsu Natural Science Foundation for Distinguished Young Scholars","award":["BK2022084"],"award-info":[{"award-number":["BK2022084"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Int. J. Mol. Sci.","IJMS"],"abstract":"<jats:p>Redox regulation plays an important role in plant stress responses. Our previous study revealed that rice GLUTATHIONE PEROXIDASE 1 (GPX1) acts as a redox sensor and transducer and promotes osmotic stress tolerance by transfer of cytosolic oxidative signals to transcription factor BASIC LEUCINE ZIPPER 68 (bZIP68). However, the mechanisms governing GPX1 activity and nuclear localization remain unclear. Here, we show that osmotic stress increases GPX1 acetylation. Peroxidase activity and subcellular localization assay indicated that the effects of acetylation on GPX1 function are site-specific, as the acetylation of K94 and K121 enhances GPX1 enzymatic activity, whereas the C-terminal K159\/K162\/K163 cluster is required for its nuclear translocation. Transgenic complementation and physiological assays confirmed that substitution of K159\/K162\/K163 sites into arginine abolished GPX1-mediated osmotic stress tolerance and the activation of bZIP68 target genes. Furthermore, we discovered that HISTONE DEACETYLASE 15 (HDA15) interacts with and deacetylates GPX1. HDA15-mediated deacetylation reduced enzymatic activity, nuclear translocation and subsequently the interaction with bZIP68 of GPX1. Accordingly, HDA15-overexpressing rice showed greater membrane damage, weaker induction of bZIP68-regulated genes and increased sensitivity to osmotic stress. These results identify HDA15-mediated GPX1 deacetylation as a negative regulatory mechanism that connects redox enzyme activity, protein localization and stress-responsive transcription in rice.<\/jats:p>","DOI":"10.3390\/ijms27167073","type":"journal-article","created":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T08:01:36Z","timestamp":1786089696000},"page":"7073","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["HDA15-Mediated Deacetylation of GPX1 Inhibits Its Nuclear Translocation and Increases Osmotic Stress Sensitivity in Rice"],"prefix":"10.3390","volume":"27","author":[{"given":"Fengchao","family":"Zhai","sequence":"first","affiliation":[{"name":"Laboratory Center of Life Sciences, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoyun","family":"Ma","sequence":"additional","affiliation":[{"name":"National Key Laboratory for the Development and Utilization of Forest Food Resources, Co-Innovation Center for Sustainable Forestry in Southern China, State Key Laboratory of Tree Genetics and Breeding, Key Laboratory of State Forestry and Grassland Administration on Subtropical Forest Biodiversity Conservation, College of Life Sciences, Nanjing Forestry University, Nanjing 210037, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wenge","family":"Li","sequence":"additional","affiliation":[{"name":"Laboratory Center of Life Sciences, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinyue","family":"Fan","sequence":"additional","affiliation":[{"name":"Laboratory Center of Life Sciences, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jing","family":"Zhang","sequence":"additional","affiliation":[{"name":"National Key Laboratory for the Development and Utilization of Forest Food Resources, Co-Innovation Center for Sustainable Forestry in Southern China, State Key Laboratory of Tree Genetics and Breeding, Key Laboratory of State Forestry and Grassland Administration on Subtropical Forest Biodiversity Conservation, College of Life Sciences, Nanjing Forestry University, Nanjing 210037, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heng","family":"Zhou","sequence":"additional","affiliation":[{"name":"Laboratory Center of Life Sciences, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3503-1267","authenticated-orcid":false,"given":"Yanjie","family":"Xie","sequence":"additional","affiliation":[{"name":"Laboratory Center of Life Sciences, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"},{"name":"National Key Laboratory for the Development and Utilization of Forest Food Resources, Co-Innovation Center for Sustainable Forestry in Southern China, State Key Laboratory of Tree Genetics and Breeding, Key Laboratory of State Forestry and Grassland Administration on Subtropical Forest Biodiversity Conservation, College of Life Sciences, Nanjing Forestry University, Nanjing 210037, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,8,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1111\/jipb.13622","article-title":"How plants sense and respond to osmotic stress","volume":"66","author":"Yu","year":"2024","journal-title":"J. Integr. Plant Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1007\/s42994-024-00195-z","article-title":"Emerging strategies to improve heat stress tolerance in crops","volume":"6","author":"Xiong","year":"2025","journal-title":"aBIOTECH"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1046\/j.1365-3040.2002.00782.x","article-title":"Molecular and genetic aspects of plant responses to osmotic stress","volume":"25","author":"Xiong","year":"2002","journal-title":"Plant Cell Environ."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/j.cell.2016.08.029","article-title":"Abiotic stress signaling and responses in plants","volume":"167","author":"Zhu","year":"2016","journal-title":"Cell"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1038\/s41477-021-00887-0","article-title":"Stress-induced reactive oxygen species compartmentalization, perception and signalling","volume":"7","author":"Castro","year":"2021","journal-title":"Nat. Plants"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1111\/tpj.13299","article-title":"Reactive oxygen species, abiotic stress and stress combination","volume":"90","author":"Choudhury","year":"2017","journal-title":"Plant J."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.1104\/pp.18.01065","article-title":"Osmotic stress activates two reactive oxygen species pathways with distinct effects on protein nanodomains and diffusion","volume":"179","author":"Fiche","year":"2019","journal-title":"Plant Physiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"3691","DOI":"10.1016\/j.molcel.2021.08.018","article-title":"Redox metabolism: ROS as specific molecular regulators of cell signaling and function","volume":"81","author":"Lennicke","year":"2021","journal-title":"Mol. Cell"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1016\/j.freeradbiomed.2022.11.019","article-title":"Plant thiol peroxidases as redox sensors and signal transducers in abiotic stress acclimation","volume":"193","author":"Vogelsang","year":"2022","journal-title":"Free Radic. Biol. Med."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1364","DOI":"10.1104\/pp.106.089458","article-title":"Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses","volume":"142","author":"Navrot","year":"2006","journal-title":"Plant Physiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.plantsci.2013.03.017","article-title":"The mitochondrial glutathione peroxidase GPX3 is essential for H2O2 homeostasis and root and shoot development in rice","volume":"208","author":"Passaia","year":"2013","journal-title":"Plant Sci."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2749","DOI":"10.1105\/tpc.106.044230","article-title":"An Arabidopsis glutathione peroxidase functions as both a redox transducer and a scavenger in abscisic acid and drought stress responses","volume":"18","author":"Miao","year":"2006","journal-title":"Plant Cell"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.molp.2021.11.006","article-title":"Rice GLUTATHIONE PEROXIDASE1-mediated oxidation of bZIP68 positively regulates ABA-independent osmotic stress signaling","volume":"15","author":"Zhou","year":"2022","journal-title":"Mol. Plant"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1104\/pp.110.171595","article-title":"Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis","volume":"155","author":"Finkemeier","year":"2011","journal-title":"Plant Physiol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1104\/pp.110.165852","article-title":"Lysine acetylation is a widespread protein modification for diverse proteins in Arabidopsis","volume":"155","author":"Wu","year":"2011","journal-title":"Plant Physiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"949","DOI":"10.15252\/msb.20177819","article-title":"Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis","volume":"13","author":"Hartl","year":"2017","journal-title":"Mol. Syst. Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1038\/s41477-025-02013-w","article-title":"Regulation of m6A RNA reader protein OsECT3 activity by lysine acetylation in the cold stress response in rice","volume":"11","author":"Ma","year":"2025","journal-title":"Nat. Plants"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"10418","DOI":"10.1073\/pnas.1521363113","article-title":"Histone deacetylase HDA6 enhances brassinosteroid signaling by inhibiting the BIN2 kinase","volume":"113","author":"Hao","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/j.molp.2019.12.011","article-title":"Histone deacetylase HDA9 and WRKY53 transcription factor are mutual antagonists in regulation of plant stress response","volume":"13","author":"Zheng","year":"2020","journal-title":"Mol. Plant"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1093\/plphys\/kiac015","article-title":"The histone deacetylase 1\/GSK3\/SHAGGY-like kinase 2\/BRASSINAZOLE-RESISTANT 1 module controls lateral root formation in rice","volume":"189","author":"Hou","year":"2022","journal-title":"Plant Physiol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"12241","DOI":"10.1093\/nar\/gkx825","article-title":"Rice NAD+-dependent histone deacetylase OsSRT1 represses glycolysis and regulates the moonlighting function of GAPDH as a transcriptional activator of glycolytic genes","volume":"45","author":"Zhang","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1093\/plcell\/koae010","article-title":"Histone deacetylase OsHDA716 represses rice chilling tolerance by deacetylating OsbZIP46 to reduce its transactivation function and protein stability","volume":"36","author":"Sun","year":"2024","journal-title":"Plant Cell"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1104\/pp.15.00533","article-title":"Binary 2in1 vectors improve in planta (co)localization and dynamic protein interaction studies","volume":"168","author":"Hecker","year":"2015","journal-title":"Plant Physiol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1038\/s41467-020-14477-9","article-title":"A RAF-SnRK2 kinase cascade mediates early osmotic stress signaling in higher plants","volume":"11","author":"Lin","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1016\/j.cell.2009.03.038","article-title":"Proteasome-mediated turnover of the transcription coactivator NPR1 plays dual roles in regulating plant immunity","volume":"137","author":"Spoel","year":"2009","journal-title":"Cell"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.chom.2015.07.005","article-title":"Post-translational modifications of the master transcriptional regulator NPR1 enable dynamic but tight control of plant immune responses","volume":"18","author":"Saleh","year":"2015","journal-title":"Cell Host Microbe"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1186\/s12964-021-00741-y","article-title":"Types of nuclear localization signals and mechanisms of protein import into the nucleus","volume":"19","author":"Lu","year":"2021","journal-title":"Cell Commun. Signal."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1111\/pce.13100","article-title":"Oxidative stress-triggered interactions between the succinyl- and acetyl-proteomes of rice leaves","volume":"41","author":"Zhou","year":"2018","journal-title":"Plant Cell Environ."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2685","DOI":"10.1021\/acschembio.6b00396","article-title":"HDAC8 Catalyzes the Hydrolysis of Long Chain Fatty Acyl Lysine","volume":"11","author":"Aramsangtienchai","year":"2016","journal-title":"ACS Chem. Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1038\/cr.2017.60","article-title":"Global profiling of crotonylation on non-histone proteins","volume":"27","author":"Xu","year":"2017","journal-title":"Cell Res."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2478","DOI":"10.2174\/1389557522666220330144151","article-title":"The Zinc-dependent HDACs: Non-histone substrates and catalytic acylation beyond deacetylation","volume":"22","author":"Zheng","year":"2022","journal-title":"Mini-Rev. Med. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"8281","DOI":"10.1073\/pnas.0602874103","article-title":"The negative regulator of plant cold responses, HOS1, is a RING E3 ligase that mediates the ubiquitination and degradation of ICE1","volume":"103","author":"Dong","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/j.devcel.2014.12.023","article-title":"OST1 kinase modulates freezing tolerance by enhancing ICE1 stability in Arabidopsis","volume":"32","author":"Ding","year":"2015","journal-title":"Dev. Cell"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1093\/mp\/sss068","article-title":"OsDMI3 is a novel component of abscisic acid signaling in the induction of antioxidant defense in leaves of rice","volume":"5","author":"Shi","year":"2012","journal-title":"Mol. Plant"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"e306","DOI":"10.21769\/BioProtoc.306","article-title":"Nuclear Extraction from Arabidopsis thaliana","volume":"2","author":"Xu","year":"2012","journal-title":"Bio-Protocol"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1111\/j.1365-313X.2008.03612.x","article-title":"Multicolor bimolecular fluorescence complementation reveals simultaneous formation of alternative CBL\/CIPK complexes in planta","volume":"56","author":"Waadt","year":"2008","journal-title":"Plant J."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/16\/7073\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,9]],"date-time":"2026-08-09T04:13:48Z","timestamp":1786248828000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/16\/7073"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,7]]},"references-count":36,"journal-issue":{"issue":"16","published-online":{"date-parts":[[2026,8]]}},"alternative-id":["ijms27167073"],"URL":"https:\/\/doi.org\/10.3390\/ijms27167073","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,7]]}}}