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Activation of the plant mevalonate pathway by extracellular ATP
The mevalonate pathway plays a critical role in multiple cellular processes in both animals and plants. In plants, the products of this pathway impact growth and development, as well as the response to environmental stress. A forward genetic screen of Arabidopsis thaliana using Ca(2+)-imaging identi...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8783019/ https://www.ncbi.nlm.nih.gov/pubmed/35064110 http://dx.doi.org/10.1038/s41467-022-28150-w |
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author | Cho, Sung-Hwan Tóth, Katalin Kim, Daewon Vo, Phuc H. Lin, Chung-Ho Handakumbura, Pubudu P. Ubach, Albert Rivas Evans, Sterling Paša-Tolić, Ljiljana Stacey, Gary |
author_facet | Cho, Sung-Hwan Tóth, Katalin Kim, Daewon Vo, Phuc H. Lin, Chung-Ho Handakumbura, Pubudu P. Ubach, Albert Rivas Evans, Sterling Paša-Tolić, Ljiljana Stacey, Gary |
author_sort | Cho, Sung-Hwan |
collection | PubMed |
description | The mevalonate pathway plays a critical role in multiple cellular processes in both animals and plants. In plants, the products of this pathway impact growth and development, as well as the response to environmental stress. A forward genetic screen of Arabidopsis thaliana using Ca(2+)-imaging identified mevalonate kinase (MVK) as a critical component of plant purinergic signaling. MVK interacts directly with the plant extracellular ATP (eATP) receptor P2K1 and is phosphorylated by P2K1 in response to eATP. Mutation of P2K1-mediated phosphorylation sites in MVK eliminates the ATP-induced cytoplasmic calcium response, MVK enzymatic activity, and suppresses pathogen defense. The data demonstrate that the plasma membrane associated P2K1 directly impacts plant cellular metabolism by phosphorylation of MVK, a key enzyme in the mevalonate pathway. The results underline the importance of purinergic signaling in plants and the ability of eATP to influence the activity of a key metabolite pathway with global effects on plant metabolism. |
format | Online Article Text |
id | pubmed-8783019 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-87830192022-02-04 Activation of the plant mevalonate pathway by extracellular ATP Cho, Sung-Hwan Tóth, Katalin Kim, Daewon Vo, Phuc H. Lin, Chung-Ho Handakumbura, Pubudu P. Ubach, Albert Rivas Evans, Sterling Paša-Tolić, Ljiljana Stacey, Gary Nat Commun Article The mevalonate pathway plays a critical role in multiple cellular processes in both animals and plants. In plants, the products of this pathway impact growth and development, as well as the response to environmental stress. A forward genetic screen of Arabidopsis thaliana using Ca(2+)-imaging identified mevalonate kinase (MVK) as a critical component of plant purinergic signaling. MVK interacts directly with the plant extracellular ATP (eATP) receptor P2K1 and is phosphorylated by P2K1 in response to eATP. Mutation of P2K1-mediated phosphorylation sites in MVK eliminates the ATP-induced cytoplasmic calcium response, MVK enzymatic activity, and suppresses pathogen defense. The data demonstrate that the plasma membrane associated P2K1 directly impacts plant cellular metabolism by phosphorylation of MVK, a key enzyme in the mevalonate pathway. The results underline the importance of purinergic signaling in plants and the ability of eATP to influence the activity of a key metabolite pathway with global effects on plant metabolism. Nature Publishing Group UK 2022-01-21 /pmc/articles/PMC8783019/ /pubmed/35064110 http://dx.doi.org/10.1038/s41467-022-28150-w Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Cho, Sung-Hwan Tóth, Katalin Kim, Daewon Vo, Phuc H. Lin, Chung-Ho Handakumbura, Pubudu P. Ubach, Albert Rivas Evans, Sterling Paša-Tolić, Ljiljana Stacey, Gary Activation of the plant mevalonate pathway by extracellular ATP |
title | Activation of the plant mevalonate pathway by extracellular ATP |
title_full | Activation of the plant mevalonate pathway by extracellular ATP |
title_fullStr | Activation of the plant mevalonate pathway by extracellular ATP |
title_full_unstemmed | Activation of the plant mevalonate pathway by extracellular ATP |
title_short | Activation of the plant mevalonate pathway by extracellular ATP |
title_sort | activation of the plant mevalonate pathway by extracellular atp |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8783019/ https://www.ncbi.nlm.nih.gov/pubmed/35064110 http://dx.doi.org/10.1038/s41467-022-28150-w |
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