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Redox state‐dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals
The evolutionarily highly conserved SNF1‐related protein kinase (SnRK1) protein kinase is a metabolic master regulator in plants, balancing the critical energy consumption between growth‐ and stress response‐related metabolic pathways. While the regulation of the mammalian [AMP‐activated protein kin...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5698759/ https://www.ncbi.nlm.nih.gov/pubmed/28940407 http://dx.doi.org/10.1002/1873-3468.12852 |
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author | Wurzinger, Bernhard Mair, Andrea Fischer‐Schrader, Katrin Nukarinen, Ella Roustan, Valentin Weckwerth, Wolfram Teige, Markus |
author_facet | Wurzinger, Bernhard Mair, Andrea Fischer‐Schrader, Katrin Nukarinen, Ella Roustan, Valentin Weckwerth, Wolfram Teige, Markus |
author_sort | Wurzinger, Bernhard |
collection | PubMed |
description | The evolutionarily highly conserved SNF1‐related protein kinase (SnRK1) protein kinase is a metabolic master regulator in plants, balancing the critical energy consumption between growth‐ and stress response‐related metabolic pathways. While the regulation of the mammalian [AMP‐activated protein kinase (AMPK)] and yeast (SNF1) orthologues of SnRK1 is well‐characterised, the regulation of SnRK1 kinase activity in plants is still an open question. Here we report that the activity and T‐loop phosphorylation of AKIN10, the kinase subunit of the SnRK1 complex, is regulated by the redox status. Although this regulation is dependent on a conserved cysteine residue, the underlying mechanism is different to the redox regulation of animal AMPK and has functional implications for the regulation of the kinase complex in plants under stress conditions. |
format | Online Article Text |
id | pubmed-5698759 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-56987592017-11-30 Redox state‐dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals Wurzinger, Bernhard Mair, Andrea Fischer‐Schrader, Katrin Nukarinen, Ella Roustan, Valentin Weckwerth, Wolfram Teige, Markus FEBS Lett Research Letters The evolutionarily highly conserved SNF1‐related protein kinase (SnRK1) protein kinase is a metabolic master regulator in plants, balancing the critical energy consumption between growth‐ and stress response‐related metabolic pathways. While the regulation of the mammalian [AMP‐activated protein kinase (AMPK)] and yeast (SNF1) orthologues of SnRK1 is well‐characterised, the regulation of SnRK1 kinase activity in plants is still an open question. Here we report that the activity and T‐loop phosphorylation of AKIN10, the kinase subunit of the SnRK1 complex, is regulated by the redox status. Although this regulation is dependent on a conserved cysteine residue, the underlying mechanism is different to the redox regulation of animal AMPK and has functional implications for the regulation of the kinase complex in plants under stress conditions. John Wiley and Sons Inc. 2017-10-04 2017-11 /pmc/articles/PMC5698759/ /pubmed/28940407 http://dx.doi.org/10.1002/1873-3468.12852 Text en © 2017 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Letters Wurzinger, Bernhard Mair, Andrea Fischer‐Schrader, Katrin Nukarinen, Ella Roustan, Valentin Weckwerth, Wolfram Teige, Markus Redox state‐dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals |
title | Redox state‐dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals |
title_full | Redox state‐dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals |
title_fullStr | Redox state‐dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals |
title_full_unstemmed | Redox state‐dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals |
title_short | Redox state‐dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals |
title_sort | redox state‐dependent modulation of plant snrk1 kinase activity differs from ampk regulation in animals |
topic | Research Letters |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5698759/ https://www.ncbi.nlm.nih.gov/pubmed/28940407 http://dx.doi.org/10.1002/1873-3468.12852 |
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