Evidence map›Paper›PMID 23178947›Full record

ArticleJournal of cell science2013

Ubiquitin-independent function of optineurin in autophagic clearance of protein aggregates.

Jelena Korac, Veronique Schaeffer, Igor Kovacevic, Albrecht M Clement, Benno Jungblut, Christian Behl, Janos Terzic, Ivan Dikic

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 181 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
181citing papers in PubMed, 1 pooled it
13.8field-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

181 citing papers in PubMed, 1 synthesis or guideline pooled it, 321 citations in OpenAlex.

  1. Guideline
  2. Trial
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Current Understanding of Protein Aggregation in Neurodegenerative Diseases.International journal of molecular sciences · 2025
    Review
  10. Article
  11. Article
  12. Mechanistic insights into the iron-sulfur cluster-dependent interaction of the autophagy receptor NCOA4 with the E3 ligase HERC2.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Evaluation of aggrephagy markers in myofibrillar myopathies.Acta neuropathologica communications · 2025
    Article
  15. Article
  16. Review
  17. The Role of the Ubiquitin System in Eye Diseases.Life (Basel, Switzerland) · 2025
    Review
  18. Review
  19. Article
  20. Review

121 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

8 authors at 4 institutions in 2 countries.

Jelena KoracDepartment of Immunology and Medical Genetics, School of Medicine, University of Split, Soltanska 2, 21000 Split, Croatia.
Veronique Schaeffer
Igor Kovacevic
Albrecht M Clement
Benno Jungblut
Christian Behl
Janos Terzic
Ivan Dikic
Goethe University Frankfurt · DEJohannes Gutenberg University Mainz · DEUniversity of Split · HRMax Planck Institute for Heart and Lung Research · DE

Funding

European Research Council 250241
6 · The paper itself

Abstract

Aggregation of misfolded proteins and the associated loss of neurons are considered a hallmark of numerous neurodegenerative diseases. Optineurin is present in protein inclusions observed in various neurodegenerative diseases including amyotrophic lateral sclerosis (ALS), Huntington's disease, Alzheimer's disease, Parkinson's disease, Creutzfeld-Jacob disease and Pick's disease. Optineurin deletion mutations have also been described in ALS patients. However, the role of optineurin in mechanisms of protein aggregation remains unclear. In this report, we demonstrate that optineurin recognizes various protein aggregates via its C-terminal coiled-coil domain in a ubiquitin-independent manner. We also show that optineurin depletion significantly increases protein aggregation in HeLa cells and that morpholino-silencing of the optineurin ortholog in zebrafish causes the motor axonopathy phenotype similar to a zebrafish model of ALS. A more severe phenotype is observed when optineurin is depleted in zebrafish carrying ALS mutations. Furthermore, TANK1 binding kinase 1 (TBK1) is colocalized with optineurin on protein aggregates and is important in clearance of protein aggregates through the autophagy-lysosome pathway. TBK1 phosphorylates optineurin at serine 177 and regulates its ability to interact with autophagy modifiers. This study provides evidence for a ubiquitin-independent function of optineurin in autophagic clearance of protein aggregates as well as additional relevance for TBK1 as an upstream regulator of the autophagic pathway.

Indexed as

AnimalsAutophagyCell Cycle ProteinsDisease Models, AnimalHeLa CellsHumansMembrane Transport ProteinsMiceMice, Inbred C57BLMice, TransgenicNeurodegenerative DiseasesPhosphorylationProtein BindingTranscription Factor TFIIIAUbiquitinZebrafishCell Cycle ProteinsMembrane Transport ProteinsOPTN protein, humanTranscription Factor TFIIIAUbiquitin

Identifiers

PMID23178947
PMCPMC3654196
OpenAlexW1985484942

What OpenQuestion holds

Textmetadata
LicenceTDM
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.