Elemental cryo-imaging reveals SOS1-dependent vacuolar sodium accumulation
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| Název: | Elemental cryo-imaging reveals SOS1-dependent vacuolar sodium accumulation |
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| Autoři: | Priya Ramakrishna, Francisco M. Gámez-Arjona, Etienne Bellani, Cristina Martin-Olmos, Stéphane Escrig, Damien De Bellis, Anna De Luca, José M. Pardo, Francisco J. Quintero, Christel Genoud, Clara Sánchez-Rodriguez, Niko Geldner, Anders Meibom |
| Přispěvatelé: | Université de Lausanne, ETH Zurich, Agencia Estatal de Investigación (España), Ministerio de Ciencia e Innovación (España), European Commission, École Polytechnique Fédérale de Lausanne, Swiss National Science Foundation, European Research Council, Ramakrishna, Priya [0000-0002-7371-6806], Gámez Arjona, Francisco M [0000-0001-5891-9843], Bellani, Etienne [0000-0003-0452-4859], Martin Olmos, Cristina [0000-0003-0688-484X], Escrig, Stéphane [0000-0001-9480-7208], De Bellis, Damien [0000-0003-3097-0465], De Luca, Anna [0000-0003-4510-8624], Pardo, José M. [0000-0001-8718-2975], Genoud, Christel [0000-0002-0933-9911], Sánchez Rodriguez, Clara [0000-0003-0987-9317], Geldner, Niko [0000-0002-2300-9644], Meibom, Anders [0000-0002-4542-2819], Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72] |
| Zdroj: | Nature Digital.CSIC. Repositorio Institucional del CSIC Consejo Superior de Investigaciones Científicas (CSIC) Nature, vol. 637, no. 8048, pp. 1228-1233 Nature, 637 (8048) |
| Informace o vydavateli: | Springer Science and Business Media LLC, 2025. |
| Rok vydání: | 2025 |
| Témata: | STRESS, Sodium-Hydrogen Exchangers, Meristem, Arabidopsis, Spectrometry, Mass, Secondary Ion, Mass, Secondary Ion, K+, SALT TOLERANCE, End hunger, achieve food security and improved nutrition and promote sustainable agriculture, Plant Roots, Article, stress, Cell Wall, PLANTS, SOS1, NA+ TRANSPORT, salt tolerance, Spectrometry, Arabidopsis Proteins, TONOPLAST, Sodium, Arabidopsis/metabolism, Sodium/metabolism, Vacuoles/metabolism, Arabidopsis Proteins/metabolism, Arabidopsis Proteins/genetics, Oryza/metabolism, Oryza/chemistry, Sodium-Hydrogen Exchangers/metabolism, Meristem/metabolism, Cell Wall/metabolism, Cell Wall/chemistry, Plant Roots/metabolism, LOCALIZATION, Oryza, transport, Vacuoles, ATPASE ACTIVITY |
| Popis: | Increasing soil salinity causes significant crop losses globally; therefore, understanding plant responses to salt (sodium) stress is of high importance. Plants avoid sodium toxicity through subcellular compartmentation by intricate processes involving a high level of elemental interdependence. Current technologies to visualize sodium, in particular, together with other elements, are either indirect or lack in resolution. Here we used the newly developed cryo nanoscale secondary ion mass spectrometry ion microprobe1, which allows high-resolution elemental imaging of cryo-preserved samples and reveals the subcellular distributions of key macronutrients and micronutrients in root meristem cells of Arabidopsis and rice. We found an unexpected, concentration-dependent change in sodium distribution, switching from sodium accumulation in the cell walls at low external sodium concentrations to vacuolar accumulation at stressful concentrations. We conclude that, in root meristems, a key function of the NHX family sodium/proton antiporter SALT OVERLY SENSITIVE 1 (also known as Na+/H+ exchanger 7; SOS1/NHX7) is to sequester sodium into vacuoles, rather than extrusion of sodium into the extracellular space. This is corroborated by the use of new genomic, complementing fluorescently tagged SOS1 variants. We show that, in addition to the plasma membrane, SOS1 strongly accumulates at late endosome/prevacuoles as well as vacuoles, supporting a role of SOS1 in vacuolar sodium sequestration. Nature, 637 (8048) ISSN:0028-0836 ISSN:1476-4687 |
| Druh dokumentu: | Article Other literature type |
| Popis souboru: | aplication/pdf; application/pdf; application/application/pdf |
| Jazyk: | English |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/s41586-024-08403-y |
| DOI: | 10.3929/ethz-b-000717087 |
| DOI: | 10.13039/501100000780 |
| DOI: | 10.13039/501100001703 |
| DOI: | 10.13039/501100004837 |
| DOI: | 10.13039/501100011033 |
| DOI: | 10.13039/501100006390 |
| DOI: | 10.13039/501100000781 |
| Přístupová URL adresa: | https://pubmed.ncbi.nlm.nih.gov/39814877 https://api.elsevier.com/content/abstract/scopus_id/85217517825 http://hdl.handle.net/10261/384397 https://serval.unil.ch/resource/serval:BIB_ABAD6C2D7A18.P001/REF.pdf https://serval.unil.ch/notice/serval:BIB_ABAD6C2D7A18 http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_ABAD6C2D7A188 http://hdl.handle.net/20.500.11850/717087 |
| Rights: | CC BY NC ND |
| Přístupové číslo: | edsair.doi.dedup.....40465cb80a6c98d46d9842502ba05a7b |
| Databáze: | OpenAIRE |
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Nájsť tento článok vo Web of Science | Abstrakt: | Increasing soil salinity causes significant crop losses globally; therefore, understanding plant responses to salt (sodium) stress is of high importance. Plants avoid sodium toxicity through subcellular compartmentation by intricate processes involving a high level of elemental interdependence. Current technologies to visualize sodium, in particular, together with other elements, are either indirect or lack in resolution. Here we used the newly developed cryo nanoscale secondary ion mass spectrometry ion microprobe1, which allows high-resolution elemental imaging of cryo-preserved samples and reveals the subcellular distributions of key macronutrients and micronutrients in root meristem cells of Arabidopsis and rice. We found an unexpected, concentration-dependent change in sodium distribution, switching from sodium accumulation in the cell walls at low external sodium concentrations to vacuolar accumulation at stressful concentrations. We conclude that, in root meristems, a key function of the NHX family sodium/proton antiporter SALT OVERLY SENSITIVE 1 (also known as Na+/H+ exchanger 7; SOS1/NHX7) is to sequester sodium into vacuoles, rather than extrusion of sodium into the extracellular space. This is corroborated by the use of new genomic, complementing fluorescently tagged SOS1 variants. We show that, in addition to the plasma membrane, SOS1 strongly accumulates at late endosome/prevacuoles as well as vacuoles, supporting a role of SOS1 in vacuolar sodium sequestration.<br />Nature, 637 (8048)<br />ISSN:0028-0836<br />ISSN:1476-4687 |
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| ISSN: | 14764687 00280836 |
| DOI: | 10.1038/s41586-024-08403-y |