Evidence map›Paper›PMID 31983282›Full record

ArticleAutophagy2020

DNA-dependent protein kinase regulates lysosomal AMP-dependent protein kinase activation and autophagy.

Pietri Puustinen, Anne Keldsbo, Elisabeth Corcelle-Termeau, Kevin Ngoei, Stine L Sønder, Thomas Farkas, Klaus Kaae Andersen, Jon S Oakhill, Marja Jäättelä

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 2 pooled it
6.2field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 2 syntheses or guidelines pooled it, 60 citations in OpenAlex.

  1. Pooled it
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  4. TRIM21 is a molecular rheostat for influenza A virus replication.bioRxiv : the preprint server for biology · 2026
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  8. NClinical and translational medicine · 2025
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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

9 authors at 3 institutions in 2 countries.

Pietri PuustinenCell Death and Metabolism Unit, Centre for Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center (DCRC) , Copenhagen, Denmark.
Anne KeldsboCell Death and Metabolism Unit, Centre for Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center (DCRC) , Copenhagen, Denmark.
Elisabeth Corcelle-TermeauCell Death and Metabolism Unit, Centre for Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center (DCRC) , Copenhagen, Denmark.
Kevin NgoeiMetabolic Signaling Laboratory, St Vincent's Institute of Medical Research and Department of Medicine, University of Melbourne , Melbourne, Australia.ORCID 0000-0003-3891-2198
Stine L SønderCell Death and Metabolism Unit, Centre for Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center (DCRC) , Copenhagen, Denmark.
Thomas FarkasCell Death and Metabolism Unit, Centre for Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center (DCRC) , Copenhagen, Denmark.
Klaus Kaae AndersenStatistics, Bioinformatics and Registry, Danish Cancer Society Research Center (DCRC) , Copenhagen, Denmark.
Jon S OakhillMetabolic Signaling Laboratory, St Vincent's Institute of Medical Research and Department of Medicine, University of Melbourne , Melbourne, Australia.
Marja JäätteläCell Death and Metabolism Unit, Centre for Autophagy, Recycling and Disease (CARD), Danish Cancer Society Research Center (DCRC) , Copenhagen, Denmark.ORCID 0000-0001-5950-7111
Danish Cancer Society · DKThe University of Melbourne · AUUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Macroautophagy/autophagy is a central component of the cytoprotective cellular stress response. To enlighten stress-induced autophagy signaling, we screened a human kinome siRNA library for regulators of autophagic flux in MCF7 human breast carcinoma cells and identified the catalytic subunit of DNA-dependent protein kinase PRKDC/DNA-PKcs as a positive regulator of basal and DNA damage-induced autophagy. Analysis of autophagy-regulating signaling cascades placed PRKDC upstream of the AMP-dependent protein kinase (AMPK) complex and ULK1 kinase. In normal culture conditions, PRKDC interacted with the AMPK complex and phosphorylated its nucleotide-sensing γ1 subunit PRKAG1/AMPKγ1 at Ser192 and Thr284, both events being significantly reduced upon the activation of the AMPK complex. Alanine substitutions of PRKDC phosphorylation sites in PRKAG1 reduced AMPK complex activation without affecting its nucleotide sensing capacity. Instead, the disturbance of PRKDC-mediated phosphorylation of PRKAG1 inhibited the lysosomal localization of the AMPK complex and its starvation-induced association with STK11 (serine/threonine kinase 11). Taken together, our data suggest that PRKDC-mediated phosphorylation of PRKAG1 primes AMPK complex to the lysosomal activation by STK11 in cancer cells thereby linking DNA damage response to autophagy and cellular metabolism.

Indexed as

AutophagyGene Expression Regulation, EnzymologicAMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesBinding SitesCell Line, TumorCytosolDNA-Activated Protein KinaseDNA DamageHumansLysosomesMCF-7 CellsPhagocytosisPhosphorylationProtein Serine-Threonine KinasesRNA, Small InterferingAMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesDNA-Activated Protein KinasePRKAG1 protein, humanPRKDC protein, humanProtein Serine-Threonine KinasesRNA, Small InterferingSTK11 protein, humanAMPKautophagylysosomemetabolismPRKDCsignaling

Identifiers

PMID31983282
PMCPMC8386596
OpenAlexW3000969248

What OpenQuestion holds

Textmetadata
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.