SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants

Detalhes bibliográficos
Autor(a) principal: Pedrotti, Lorenzo
Data de Publicação: 2015
Outros Autores: 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
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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spelling 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)
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