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Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivation

2016-08-22Journal article Open access
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dc.contributor.authorNukarinen, Ella
dc.contributor.authorNägele, Thomas
dc.contributor.authorPedrotti, Lorenzo
dc.contributor.authorWurzinger, Bernhard
dc.contributor.authorMair, Andrea
dc.contributor.authorLandgraf, Ramona
dc.contributor.authorBörnke, Frederik
dc.contributor.authorHanson, Johannes
dc.contributor.authorTeige, Markus
dc.contributor.authorBaena-Gonzalez, Elena
dc.contributor.authorDröge-Laser, Wolfgang
dc.contributor.authorWeckwerth, Wolfram
dc.date.accessioned2016-08-29T11:53:04Z
dc.date.available2016-08-29T11:53:04Z
dc.date.issued2016-08-22
dc.description.abstractSince years, research on SnRK1, the major cellular energy sensor in plants, has tried to define its role in energy signalling. However, these attempts were notoriously hampered by the lethality of a complete knockout of SnRK1. Therefore, we generated an inducible amiRNA::SnRK1α2 in a snrk1α1 knock out background (snrk1α1/α2) to abolish SnRK1 activity to understand major systemic functions of SnRK1 signalling under energy deprivation triggered by extended night treatment. We analysed the in vivo phosphoproteome, proteome and metabolome and found that activation of SnRK1 is essential for repression of high energy demanding cell processes such as protein synthesis. The most abundant effect was the constitutively high phosphorylation of ribosomal protein S6 (RPS6) in the snrk1α1/α2 mutant. RPS6 is a major target of TOR signalling and its phosphorylation correlates with translation. Further evidence for an antagonistic SnRK1 and TOR crosstalk comparable to the animal system was demonstrated by the in vivo interaction of SnRK1α1 and RAPTOR1B in the cytosol and by phosphorylation of RAPTOR1B by SnRK1α1 in kinase assays. Moreover, changed levels of phosphorylation states of several chloroplastic proteins in the snrk1α1/α2 mutant indicated an unexpected link to regulation of photosynthesis, the main energy source in plants.pt_PT
dc.description.sponsorshipAustrian Science Fund FWF Projects: (P 26342, P 25488, P 28491).pt_PT
dc.identifier.citationNukarinen, E. et al. Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivation. Sci. Rep. 6, 31697; doi: 10.1038/srep31697 (2016).pt_PT
dc.identifier.doi10.1038/srep31697pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/694
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherNature Publishing Grouppt_PT
dc.relationMetabolic Reprogramming by Induction of Transcription
dc.relation.publisherversionhttp://www.nature.com/articles/srep31697pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectPlant signallingpt_PT
dc.subjectSystems analysispt_PT
dc.titleQuantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivationpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleMetabolic Reprogramming by Induction of Transcription
oaire.awardURIinfo:eu-repo/grantAgreement/EC/FP7/264474/EU
oaire.citation.endPage19pt_PT
oaire.citation.startPage1pt_PT
oaire.citation.titleScientific Reportspt_PT
oaire.citation.volume6pt_PT
oaire.fundingStreamFP7
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameEuropean Commission
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublicationcf6c4467-aeee-4b37-ac24-10f8395a9d85
relation.isProjectOfPublication.latestForDiscoverycf6c4467-aeee-4b37-ac24-10f8395a9d85

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