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A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process
Phototropins are light-activated protein kinases, which contribute to photosynthesis optimization both through enhancement of photon absorption when light is limiting and avoidance responses in high light. This duality is in part endowed by the presence of phototropins with different photosensitivit...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6008296/ https://www.ncbi.nlm.nih.gov/pubmed/29921904 http://dx.doi.org/10.1038/s41467-018-04752-1 |
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author | Schumacher, Paolo Demarsy, Emilie Waridel, Patrice Petrolati, Laure Allenbach Trevisan, Martine Fankhauser, Christian |
author_facet | Schumacher, Paolo Demarsy, Emilie Waridel, Patrice Petrolati, Laure Allenbach Trevisan, Martine Fankhauser, Christian |
author_sort | Schumacher, Paolo |
collection | PubMed |
description | Phototropins are light-activated protein kinases, which contribute to photosynthesis optimization both through enhancement of photon absorption when light is limiting and avoidance responses in high light. This duality is in part endowed by the presence of phototropins with different photosensitivity (phot1 and phot2). Here we show that phot1, which senses low light to promote positive phototropism (growth towards the light), also limits the response in high light. This response depends in part on phot1-mediated phosphorylation of Phytochrome Kinase Substrate 4 (PKS4). This light-regulated phosphorylation switch changes PKS4 from a phototropism enhancer in low light to a factor limiting the process in high light. In such conditions phot1 and PKS4 phosphorylation prevent phototropic responses to shallow light gradients and limit phototropism in a natural high light environment. Hence, by modifying PKS4 activity in high light the phot1-PKS4 regulon enables appropriate physiological adaptations over a range of light intensities. |
format | Online Article Text |
id | pubmed-6008296 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-60082962018-06-21 A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process Schumacher, Paolo Demarsy, Emilie Waridel, Patrice Petrolati, Laure Allenbach Trevisan, Martine Fankhauser, Christian Nat Commun Article Phototropins are light-activated protein kinases, which contribute to photosynthesis optimization both through enhancement of photon absorption when light is limiting and avoidance responses in high light. This duality is in part endowed by the presence of phototropins with different photosensitivity (phot1 and phot2). Here we show that phot1, which senses low light to promote positive phototropism (growth towards the light), also limits the response in high light. This response depends in part on phot1-mediated phosphorylation of Phytochrome Kinase Substrate 4 (PKS4). This light-regulated phosphorylation switch changes PKS4 from a phototropism enhancer in low light to a factor limiting the process in high light. In such conditions phot1 and PKS4 phosphorylation prevent phototropic responses to shallow light gradients and limit phototropism in a natural high light environment. Hence, by modifying PKS4 activity in high light the phot1-PKS4 regulon enables appropriate physiological adaptations over a range of light intensities. Nature Publishing Group UK 2018-06-19 /pmc/articles/PMC6008296/ /pubmed/29921904 http://dx.doi.org/10.1038/s41467-018-04752-1 Text en © The Author(s) 2018 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/. |
spellingShingle | Article Schumacher, Paolo Demarsy, Emilie Waridel, Patrice Petrolati, Laure Allenbach Trevisan, Martine Fankhauser, Christian A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process |
title | A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process |
title_full | A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process |
title_fullStr | A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process |
title_full_unstemmed | A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process |
title_short | A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process |
title_sort | phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6008296/ https://www.ncbi.nlm.nih.gov/pubmed/29921904 http://dx.doi.org/10.1038/s41467-018-04752-1 |
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