Evidence map›Paper›PMID 34226595›Full record

ArticleScientific reports2021

FIP200 controls the TBK1 activation threshold at SQSTM1/p62-positive condensates.

David Schlütermann, Niklas Berleth, Jana Deitersen, Nora Wallot-Hieke, Olena Friesen, Wenxian Wu, Fabian Stuhldreier, Yadong Sun, Lena Berning, Annabelle Friedrich and 7 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
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  4. Article
  5. TBK1 restricts IRGQ-mediated autophagy.Nature communications · 2026
    Article
  6. Review
  7. Review
  8. Article
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  10. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
    Review
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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

17 authors at 2 institutions in 1 country.

David SchlütermannInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Niklas BerlethInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Jana DeitersenInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Nora Wallot-HiekeInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Olena FriesenInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Wenxian WuInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Fabian StuhldreierInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Yadong SunInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Lena BerningInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Annabelle FriedrichInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
María José MendiburoInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Christoph PeterInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Constanze WiekDepartment of Otorhinolaryngology and Head/Neck Surgery, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225, Düsseldorf, Germany.
Helmut HanenbergDepartment of Otorhinolaryngology and Head/Neck Surgery, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, 40225, Düsseldorf, Germany.
Anja StefanskiMolecular Proteomics Laboratory, Biologisch-Medizinisches Forschungszentrum (BMFZ), Heinrich Heine University Düsseldorf, 40225, Düsseldorf, Germany.
Kai StühlerInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany.
Björn StorkInstitute of Molecular Medicine I, Medical Faculty, University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Universitätsstr. 1, Building 22.03, 40225, Düsseldorf, Germany. bjoern.stork@hhu.de.
Heinrich Heine University Düsseldorf · DEDüsseldorf University Hospital · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein kinase TBK1 is a central regulator of innate immune responses and autophagy, and ablation of either function has been linked to neuroinflammatory or degenerative diseases. Autophagy is an intracellular process that recycles old or damaged proteins and organelles. In recent years, the TBK1-dependent regulation of autophagy pathways has been characterized. However, the autophagy-dependent regulation of TBK1 activity awaits further clarification. Here, we observed that TBK1 is recruited to SQSTM1/p62-containing aggregates via the selective autophagy receptor TAX1BP1. In these aggregates, TBK1 phosphorylates SQSTM1/p62 at serine 403 and thus presumably regulates the efficient engulfment and clearance of these structures. We found that TBK1 activation is strongly increased if FIP200, a component of the autophagy-inducing ULK1 complex, is not present or cannot bind to TAX1BP1. Given our collective findings, we hypothesize that FIP200 ensures the inducible activation of TBK1 at SQSTM1/p62 condensates.

Indexed as

AutophagyAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsHumansImmunity, InnateIntracellular Signaling Peptides and ProteinsNeoplasm ProteinsNeurodegenerative DiseasesPhosphorylationProtein Serine-Threonine KinasesSequestosome-1 ProteinSignal TransductionAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsIntracellular Signaling Peptides and ProteinsNeoplasm ProteinsProtein Serine-Threonine KinasesRB1CC1 protein, humanSequestosome-1 ProteinSQSTM1 protein, humanTAX1BP1 protein, humanTBK1 protein, human

Identifiers

PMID34226595
PMCPMC8257712
OpenAlexW3180968677

What OpenQuestion holds

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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.