Evidence map›Paper›PMID 34471133›Full record

ArticleNature communications2021

Reconstitution defines the roles of p62, NBR1 and TAX1BP1 in ubiquitin condensate formation and autophagy initiation.

Eleonora Turco, Adriana Savova, Flora Gere, Luca Ferrari, Julia Romanov, Martina Schuschnig, Sascha Martens

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
145citing papers in PubMed, 1 pooled it
23.5field-weighted citation impact, top 1% 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

145 citing papers in PubMed, 1 synthesis or guideline pooled it, 227 citations in OpenAlex.

  1. Pooled it
  2. Regulation and roles of mammalian mitophagy.Nature reviews. Molecular cell biology · 2026
    Review
  3. Review
  4. Mitophagy coordinates organelle crosstalk in health and diseases.Signal transduction and targeted therapy · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. ADSCs-Exo ameliorates UVB-induced skin DNA damage via p62-RNF168-dependent histone ubiquitination.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. TBK1 restricts IRGQ-mediated autophagy.Nature communications · 2026
    Article
  19. Review
  20. Mitophagy in kidney transplantation ischemia-reperfusion injury.International urology and nephrology · 2026
    Review

85 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

7 authors at 1 institution in 1 country.

Eleonora Turco *Max Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria. eleonora.turco@univie.ac.at.ORCID 0000-0002-5266-4592
Adriana Savova *Max Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
Flora GereMax Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
Luca FerrariMax Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
Julia RomanovMax Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
Martina SchuschnigMax Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
Sascha MartensMax Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria. sascha.martens@univie.ac.at.ORCID 0000-0003-3786-8199
University of Vienna · AT

Funding

Austrian Science Fund FWF P 30401Austrian Science Fund FWF W 1261
6 · The paper itself

Abstract

The autophagic degradation of misfolded and ubiquitinated proteins is important for cellular homeostasis. In this process, which is governed by cargo receptors, ubiquitinated proteins are condensed into larger structures and subsequently become targets for the autophagy machinery. Here we employ in vitro reconstitution and cell biology to define the roles of the human cargo receptors p62/SQSTM1, NBR1 and TAX1BP1 in the selective autophagy of ubiquitinated substrates. We show that p62 is the major driver of ubiquitin condensate formation. NBR1 promotes condensate formation by equipping the p62-NBR1 heterooligomeric complex with a high-affinity UBA domain. Additionally, NBR1 recruits TAX1BP1 to the ubiquitin condensates formed by p62. While all three receptors interact with FIP200, TAX1BP1 is the main driver of FIP200 recruitment and thus the autophagic degradation of p62-ubiquitin condensates. In summary, our study defines the roles of all three receptors in the selective autophagy of ubiquitin condensates.

Indexed as

AutophagyAutophagy-Related ProteinsCarrier ProteinsCell LineHumansIntracellular Signaling Peptides and ProteinsNeoplasm ProteinsProtein DomainsRNA-Binding ProteinsSequestosome-1 ProteinUbiquitinUbiquitinated ProteinsAutophagy-Related ProteinsCarrier ProteinsIntracellular Signaling Peptides and ProteinsNBR1 protein, humanNeoplasm ProteinsP62 protein, humanRB1CC1 protein, humanRNA-Binding ProteinsSequestosome-1 ProteinSQSTM1 protein, humanTAX1BP1 protein, humanUbiquitinUbiquitinated Proteins

Identifiers

PMID34471133
PMCPMC8410870
OpenAlexW3197867551

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.