Evidence map›Paper›PMID 22895009›Full record

ArticleCell cycle (Georgetown, Tex.)2012

CEP192 interacts physically and functionally with the K63-deubiquitinase CYLD to promote mitotic spindle assembly.

Maria Ana Gomez-Ferreria, Mikhail Bashkurov, Michael Mullin, Anne-Claude Gingras, Laurence Pelletier

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. AKT and DUBs: a bidirectional relationship.Cellular & molecular biology letters · 2025
    Review
  4. Article
  5. Article
  6. CYLD in health and disease.Disease models & mechanisms · 2023
    Review
  7. Ttc30a affects tubulin modifications in a model for ciliary chondrodysplasia with polycystic kidney disease.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Targeting E3 Ubiquitin Ligases and Deubiquitinases in Ciliopathy and Cancer.International journal of molecular sciences · 2020
    Review
  9. The Role of Deubiquitinating Enzymes in the Various Forms of Autophagy.International journal of molecular sciences · 2020
    Review
  10. Deubiquitinating Enzymes: A Critical Regulator of Mitosis.International journal of molecular sciences · 2019
    Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. CYLD-mediated signaling and diseases.Current drug targets · 2015
    Review
  19. Article
  20. Article
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 1 institution in 1 country.

Maria Ana Gomez-FerreriaSamuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.
Mikhail Bashkurov
Michael Mullin
Anne-Claude Gingras
Laurence Pelletier
Mount Sinai Hospital · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CEP192 is a centrosome protein that plays a critical role in centrosome biogenesis and function in mammals, Drosophila and C. elegans. Moreover, CEP192-depleted cells arrest in mitosis with disorganized microtubules, suggesting that CEP192's function in spindle assembly goes beyond its role in centrosome activity and pointing to a potentially more direct role in the regulation of the mitotic microtubule landscape. To better understand CEP192 function in mitosis, we used mass spectrometry to identify CEP192-interacting proteins. We previously reported that CEP192 interacts with NEDD1, a protein that associates with the γ-tubulin ring complex (γ-TuRC) and regulates its phosphorylation status during mitosis. Additionally, within the array of proteins that interact with CEP192, we identified the microtubule binding K63-deubiquitinase CYLD. Further analyses show that co-depletion of CYLD alleviates the bipolar spindle assembly defects observed in CEP192-depleted cells. This functional relationship exposes an intriguing role for CYLD in spindle formation and raises the tantalizing possibility that CEP192 promotes robust mitotic spindle assembly by regulating K63-polyubiquitin-mediated signaling through CYLD.

Indexed as

Chromosomal Proteins, Non-HistoneDeubiquitinating Enzyme CYLDHEK293 CellsHeLa CellsHumansImmunoprecipitationLysineMass SpectrometryProtein BindingSpindle ApparatusTumor Suppressor ProteinsCep192 protein, humanChromosomal Proteins, Non-HistoneCYLD protein, humanDeubiquitinating Enzyme CYLDLysineTumor Suppressor Proteins

Identifiers

PMID22895009
PMCPMC3478306
OpenAlexW2070007414

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.