Evidence map›Paper›PMID 31805502›Full record

ArticleRedox biology2020

AMPK leads to phosphorylation of the transcription factor Nrf2, tuning transactivation of selected target genes.

Manuel Matzinger, Katrin Fischhuber, Daniel Pölöske, Karl Mechtler, Elke H Heiss

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
4.5field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

81 citing papers in PubMed, 132 citations in OpenAlex.

  1. Article
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  13. Spatial regulation of AMPK activity under oxidative stress requires LKB1.bioRxiv : the preprint server for biology · 2025
    Article
  14. Transcriptional Repression of CCL2 by KInternational journal of molecular sciences · 2025
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  16. Review
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  20. Fucoxanthin fromMarine drugs · 2025
    Article

21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Manuel MatzingerDepartment of Pharmacognosy, University of Vienna, Vienna, Austria; Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.
Katrin FischhuberDepartment of Pharmacognosy, University of Vienna, Vienna, Austria.
Daniel PölöskeDepartment of Pharmacognosy, University of Vienna, Vienna, Austria.
Karl MechtlerInstitute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria; Institute of Molecular Biotechnology, Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Elke H HeissDepartment of Pharmacognosy, University of Vienna, Vienna, Austria. Electronic address: elke.heiss@univie.ac.at.
University of Vienna · ATVienna Biocenter · AT

Funding

Austrian Science Fund FWF I 3686Austrian Science Fund FWF P 29392
6 · The paper itself

Abstract

The transcription factor Nrf2 (nuclear factor (erythroid-derived 2)-like 2) and the kinase AMPK (AMP-activated protein kinase) participate in the cellular adaptive response to redox or energy stress. Despite accumulating evidence for positive cooperativity between both proteins, information about direct post-translational modification of Nrf2 by AMPK in living cells is scarce. Here, MS-based analysis of immunoprecipitated Nrf2 revealed serine 374, 408 and 433 in human Nrf2 to be hyperphosphorylated as a function of activated AMPK. A direct phosphate-transfer by AMPK to those sites was indicated by in vitro kinase assays with recombinant proteins as well as interaction of AMPK and Nrf2 in cells, evident by co-immunoprecipitation. Mutation of serine 374, 408 and 433 to alanine did not markedly affect half-life, nuclear accumulation or induction of reporter gene expression upon Nrf2 activation with sulforaphane. However, some selected endogenous Nrf2 target genes responded with decreased induction when the identified phosphosites were mutated, whereas others remained unaffected. Notably, the genes susceptible to the mutation of the phosphorylation sites in Nrf2 consistently showed reduced induction in AMPKα1 -/-cells. Overall, our data reveal AMPK-triggered phosphorylation of Nrf2 at three serine residues, apparently determining the extent of transactivation of selected target genes.

Indexed as

AMP-Activated Protein KinasesNF-E2-Related Factor 2Gene Expression RegulationHumansPhosphorylationTranscriptional ActivationAMP-Activated Protein KinasesNF-E2-Related Factor 2AMPKNFE2L2Nrf2PhosphorylationProteomicsTranscription factor

Identifiers

PMID31805502
PMCPMC6909106
OpenAlexW2991041523

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.