SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.7/608 |
Resumo: | Metabolic adjustment to changing environmental conditions, particularly balancing of growth and defense responses, is crucial for all organisms to survive. The evolutionary conserved AMPK/Snf1/SnRK1 kinases are well-known metabolic master regulators in the low-energy response in animals, yeast and plants. They act at two different levels: by modulating the activity of key metabolic enzymes, and by massive transcriptional reprogramming. While the first part is well established, the latter function is only partially understood in animals and not at all in plants. Here we identified the Arabidopsis transcription factor bZIP63 as key regulator of the starvation response and direct target of the SnRK1 kinase. Phosphorylation of bZIP63 by SnRK1 changed its dimerization preference, thereby affecting target gene expression and ultimately primary metabolism. A bzip63 knock-out mutant exhibited starvation-related phenotypes, which could be functionally complemented by wild type bZIP63, but not by a version harboring point mutations in the identified SnRK1 target sites. |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plantsAdaptation, PhysiologicalArabidopsisArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsGene Knockout TechniquesGenetic Complementation TestPhosphorylationProtein Processing, Post-TranslationalProtein-Serine-Threonine KinasesGene Expression Regulation, PlantProtein MultimerizationMetabolic adjustment to changing environmental conditions, particularly balancing of growth and defense responses, is crucial for all organisms to survive. The evolutionary conserved AMPK/Snf1/SnRK1 kinases are well-known metabolic master regulators in the low-energy response in animals, yeast and plants. They act at two different levels: by modulating the activity of key metabolic enzymes, and by massive transcriptional reprogramming. While the first part is well established, the latter function is only partially understood in animals and not at all in plants. Here we identified the Arabidopsis transcription factor bZIP63 as key regulator of the starvation response and direct target of the SnRK1 kinase. Phosphorylation of bZIP63 by SnRK1 changed its dimerization preference, thereby affecting target gene expression and ultimately primary metabolism. A bzip63 knock-out mutant exhibited starvation-related phenotypes, which could be functionally complemented by wild type bZIP63, but not by a version harboring point mutations in the identified SnRK1 target sites.Austrian Science Fund (FWF) grant: (P23435); Deutsche Forschungsgemeinschaft grant (HA2146/8-2); FCT grants: (PTDC/BIA-PLA/3937/2012, UID/Multi/0455½013).Elife Sciences PublicationsARCAPedrotti, LorenzoWurzinger, BernhardAnrather, DorotheaSimeunovic, AndreaWeiste, ChristophValerio, ConcettaDietrich, KatrinKirchler, TobiasNägele, ThomasVicente Carbajosa, JesúsHanson, JohannesBaena-González, ElenaChaban, ChristinaWeckwerth, WolframDröge-Laser, WolfgangTeige, Markus2016-05-17T15:19:03Z2015-08-112015-08-11T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfapplication/pdfhttp://hdl.handle.net/10400.7/608engeLife 2015;4:e0582810.7554/eLife.05828info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2022-11-29T14:34:59ZPortal AgregadorONG |
dc.title.none.fl_str_mv |
SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants |
title |
SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants |
spellingShingle |
SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants Pedrotti, Lorenzo Adaptation, Physiological Arabidopsis Arabidopsis Proteins Basic-Leucine Zipper Transcription Factors Gene Knockout Techniques Genetic Complementation Test Phosphorylation Protein Processing, Post-Translational Protein-Serine-Threonine Kinases Gene Expression Regulation, Plant Protein Multimerization |
title_short |
SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants |
title_full |
SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants |
title_fullStr |
SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants |
title_full_unstemmed |
SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants |
title_sort |
SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants |
author |
Pedrotti, Lorenzo |
author_facet |
Pedrotti, Lorenzo Wurzinger, Bernhard Anrather, Dorothea Simeunovic, Andrea Weiste, Christoph Valerio, Concetta Dietrich, Katrin Kirchler, Tobias Nägele, Thomas Vicente Carbajosa, Jesús Hanson, Johannes Baena-González, Elena Chaban, Christina Weckwerth, Wolfram Dröge-Laser, Wolfgang Teige, Markus |
author_role |
author |
author2 |
Wurzinger, Bernhard Anrather, Dorothea Simeunovic, Andrea Weiste, Christoph Valerio, Concetta Dietrich, Katrin Kirchler, Tobias Nägele, Thomas Vicente Carbajosa, Jesús Hanson, Johannes Baena-González, Elena Chaban, Christina Weckwerth, Wolfram Dröge-Laser, Wolfgang Teige, Markus |
author2_role |
author author author author author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
ARCA |
dc.contributor.author.fl_str_mv |
Pedrotti, Lorenzo Wurzinger, Bernhard Anrather, Dorothea Simeunovic, Andrea Weiste, Christoph Valerio, Concetta Dietrich, Katrin Kirchler, Tobias Nägele, Thomas Vicente Carbajosa, Jesús Hanson, Johannes Baena-González, Elena Chaban, Christina Weckwerth, Wolfram Dröge-Laser, Wolfgang Teige, Markus |
dc.subject.por.fl_str_mv |
Adaptation, Physiological Arabidopsis Arabidopsis Proteins Basic-Leucine Zipper Transcription Factors Gene Knockout Techniques Genetic Complementation Test Phosphorylation Protein Processing, Post-Translational Protein-Serine-Threonine Kinases Gene Expression Regulation, Plant Protein Multimerization |
topic |
Adaptation, Physiological Arabidopsis Arabidopsis Proteins Basic-Leucine Zipper Transcription Factors Gene Knockout Techniques Genetic Complementation Test Phosphorylation Protein Processing, Post-Translational Protein-Serine-Threonine Kinases Gene Expression Regulation, Plant Protein Multimerization |
description |
Metabolic adjustment to changing environmental conditions, particularly balancing of growth and defense responses, is crucial for all organisms to survive. The evolutionary conserved AMPK/Snf1/SnRK1 kinases are well-known metabolic master regulators in the low-energy response in animals, yeast and plants. They act at two different levels: by modulating the activity of key metabolic enzymes, and by massive transcriptional reprogramming. While the first part is well established, the latter function is only partially understood in animals and not at all in plants. Here we identified the Arabidopsis transcription factor bZIP63 as key regulator of the starvation response and direct target of the SnRK1 kinase. Phosphorylation of bZIP63 by SnRK1 changed its dimerization preference, thereby affecting target gene expression and ultimately primary metabolism. A bzip63 knock-out mutant exhibited starvation-related phenotypes, which could be functionally complemented by wild type bZIP63, but not by a version harboring point mutations in the identified SnRK1 target sites. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-08-11 2015-08-11T00:00:00Z 2016-05-17T15:19:03Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.7/608 |
url |
http://hdl.handle.net/10400.7/608 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
eLife 2015;4:e05828 10.7554/eLife.05828 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elife Sciences Publications |
publisher.none.fl_str_mv |
Elife Sciences Publications |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
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repository.mail.fl_str_mv |
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1777301593787465728 |