Evidence map›Paper›PMID 26234217›Full record

ArticleCurrent biology : CB2015

Zeta-Tubulin Is a Member of a Conserved Tubulin Module and Is a Component of the Centriolar Basal Foot in Multiciliated Cells.

Erin Turk, Airon A Wills, Taejoon Kwon, Jakub Sedzinski, John B Wallingford, Tim Stearns

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Actin cytoskeletal regulation of ciliogenesis in development and disease.Developmental dynamics : an official publication of the American Association of Anatomists · 2024
    Review
  6. Article
  7. Pathogenic variants in autism geneProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
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  11. Article
  12. Basal bodies bend in response to ciliary forces.Molecular biology of the cell · 2022
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
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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

6 authors at 3 institutions in 1 country.

Erin TurkDepartment of Biology, Stanford University, Stanford, CA 94305, USA.
Airon A WillsDepartment of Molecular Biosciences and Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, TX 78712, USA.
Taejoon KwonDepartment of Molecular Biosciences and Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, TX 78712, USA.
Jakub SedzinskiDepartment of Molecular Biosciences and Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, TX 78712, USA.
John B WallingfordDepartment of Molecular Biosciences and Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, TX 78712, USA; Howard Hughes Medical Institute.
Tim StearnsDepartment of Biology, Stanford University, Stanford, CA 94305, USA; Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: stearns@stanford.edu.
The University of Texas at Austin · USStanford University · USHoward Hughes Medical Institute · US

Funding

Leveraging innovative technologies in basic and clinical cancer researchT32CA009302 · NCI · STANFORD UNIVERSITY · PI LAURA D ATTARDI, Aaron M Newman · 1985 to 2026
$19.1M
GAMMA TUBULIN AND CENTROSOME STRUCTURE AND FUNCTIONR01GM052022 · NIGMS · STANFORD UNIVERSITY · PI STEARNS, TIM · 1995 to 2017
$6.5M
Development and function in mucociliary epitheliaR01HL117164 · NHLBI · UNIVERSITY OF TEXAS AT AUSTIN · PI John B Wallingford · 2013 to 2026
$4.7M
Transmission Electron MicroscopeS10RR026780 · NCRR · STANFORD UNIVERSITY · PI TALBOT, WILLIAM S · 2010 to 2010
$412k
Mechanisms of primary cilia disassembly in proliferating neuroepithelial cellsF32GM103146 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI WILLS, AIRON A · 2012 to 2014
$169k
NCI NIH HHS T32 CA009302NCI NIH HHS T32 CA09302NCRR NIH HHS 1S10RR026780-01NCRR NIH HHS S10 RR026780NHLBI NIH HHS R01 HL117164NHLBI NIH HHS R01HL117164NIGMS NIH HHS F32 GM103146NIGMS NIH HHS F32GM103146NIGMS NIH HHS R01 GM052022NIGMS NIH HHS R01GM052022
6 · The paper itself

Abstract

There are six members of the tubulin superfamily in eukaryotes. Alpha- and beta-tubulin form a heterodimer that polymerizes to form microtubules, and gamma-tubulin nucleates microtubules as a component of the gamma-tubulin ring complex. Alpha-, beta-, and gamma-tubulin are conserved in all eukaryotes. In contrast, delta- and epsilon-tubulin are conserved in many, but not all, eukaryotes and are associated with centrioles, although their molecular function is unclear. Zeta-tubulin is the sixth and final member of the tubulin superfamily and is largely uncharacterized. We find that zeta-, epsilon-, and delta-tubulin form an evolutionarily co-conserved module, the ZED module, that has been lost at several junctions in eukaryotic evolution and that zeta- and delta-tubulin are evolutionarily interchangeable. Humans lack zeta-tubulin but have delta-tubulin. In Xenopus multiciliated cells, zeta-tubulin is a component of the basal foot, a centriolar appendage that connects centrioles to the apical cytoskeleton, and co-localizes there with epsilon-tubulin. Depletion of zeta-tubulin results in disorganization of centriole distribution and polarity in multiciliated cells. In contrast with multiciliated cells, zeta-tubulin in cycling cells does not localize to centrioles and is associated with the TRiC/CCT cytoplasmic chaperone complex. We conclude that zeta-tubulin facilitates interactions between the centrioles and the apical cytoskeleton as a component of the basal foot in differentiated cells and propose that the ZED tubulins are important for centriole functionalization and orientation of centrioles with respect to cellular polarity axes.

Indexed as

AnimalsCentriolesCytoskeletonTubulinXenopus laevisXenopus ProteinsTubulinXenopus Proteins

Identifiers

PMID26234217
PMCPMC4546511
OpenAlexW1778323036

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.