Evidence map›Paper›PMID 30893853›Full record

ReviewCells2019

Microtubular and Nuclear Functions of γ-Tubulin: Are They LINCed?

Jana Chumová, Hana Kourová, Lucie Trögelová, Petr Halada, Pavla Binarová

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Identification of candidate nucleomodulins in ESKAPE bacteria -Frontiers in cellular and infection microbiology · 2026
    Article
  4. Article
  5. A transient radial cortical microtubule array primes cell division inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022
    Review
  8. Review
  9. Review
  10. OncoTargets and therapy · 2021
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. The Biology of the Nuclear Envelope and Its Implications in Cancer Biology.International journal of molecular sciences · 2019
    Review
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.

Jana ChumováInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech Republic. jana.chumova@biomed.cas.cz.
Hana KourováInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech Republic. kourova@biomed.cas.cz.
Lucie TrögelováInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech Republic. lucie.trogelova@biomed.cas.cz.
Petr HaladaInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech Republic. halada@biomed.cas.cz.
Pavla BinarováInstitute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, 142 20 Prague, Czech Republic. binarova@biomed.cas.cz.ORCID 0000-0002-7203-2250
Czech Academy of Sciences · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

γ-Tubulin is a conserved member of the tubulin superfamily with a function in microtubule nucleation. Proteins of γ-tubulin complexes serve as nucleation templates as well as a majority of other proteins contributing to centrosomal and non-centrosomal nucleation, conserved across eukaryotes. There is a growing amount of evidence of γ-tubulin functions besides microtubule nucleation in transcription, DNA damage response, chromatin remodeling, and on its interactions with tumor suppressors. However, the molecular mechanisms are not well understood. Furthermore, interactions with lamin and SUN proteins of the LINC complex suggest the role of γ-tubulin in the coupling of nuclear organization with cytoskeletons. γ-Tubulin that belongs to the clade of eukaryotic tubulins shows characteristics of both prokaryotic and eukaryotic tubulins. Both human and plant γ-tubulins preserve the ability of prokaryotic tubulins to assemble filaments and higher-order fibrillar networks. γ-Tubulin filaments, with bundling and aggregating capacity, are suggested to perform complex scaffolding and sequestration functions. In this review, we discuss a plethora of γ-tubulin molecular interactions and cellular functions, as well as recent advances in understanding the molecular mechanisms behind them.

Indexed as

AnimalsCell CycleCell NucleusHumansMicrotubulesNuclear EnvelopeNuclear ProteinsTubulinNuclear ProteinsTubulinfilamentsgamma-tubulinlaminsmechanosensingnuclear functionsnucleationSUN proteins

Identifiers

PMID30893853
PMCPMC6468392
OpenAlexW2924756171

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.