Evidence map›Paper›PMID 23704354›Full record

ArticleJournal of cell science2013

ε-tubulin is essential in Tetrahymena thermophila for the assembly and stability of basal bodies.

Ian Ross, Christina Clarissa, Thomas H Giddings, Mark Winey

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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mitotic Poisons in Research and Medicine.Molecules (Basel, Switzerland) · 2020
    Review
  7. Article
  8. The Structural and Molecular Underpinnings of Gametogenesis inFrontiers in cellular and infection microbiology · 2020
    Review
  9. Motile Cilia: Innovation and Insight From Ciliate Model Organisms.Frontiers in cell and developmental biology · 2019
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. The ABCs of Centriole Architecture: The Form and Function of Triplet Microtubules.Cold Spring Harbor symposia on quantitative biology · 2017
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Ian RossDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado-Boulder, Boulder, CO 80309, USA.
Christina Clarissa
Thomas H Giddings
Mark Winey
University of Colorado Boulder · US

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BABBITT, PATRICIA CLEMENT · 1985 to 2011
$17.6M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
TRAINING IN SIGNAL TRANSDUCTION &CELL CYCLE REGULATIONT32GM008759 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI AHN, NATALIE G. · 2000 to 2020
$5.9M
Predoctoral Training Program in Signaling and Cellular Regulation INCLUDE Down Syndrome SupplementT32GM142607 · NIGMS · UNIVERSITY OF COLORADO · PI Sabrina Leigh Spencer, Tin Tin Su · 2021 to 2026
$3.6M
Tetrahymena Basal Body DuplicationR01GM074746 · NIGMS · UNIVERSITY OF COLORADO · PI WINEY, MARK · 2006 to 2015
$3.0M
NCRR NIH HHS 2P41RR001081NCRR NIH HHS P41 RR001081NIGMS NIH HHS 9P41GM103311NIGMS NIH HHS P41 GM103311NIGMS NIH HHS R01 GM074746NIGMS NIH HHS T32 GM008759NIGMS NIH HHS T32 GM08759NIGMS NIH HHS T32 GM142607
6 · The paper itself

Abstract

Basal bodies and centrioles are conserved microtubule-based organelles the improper assembly of which leads to a number of diseases, including ciliopathies and cancer. Tubulin family members are conserved components of these structures that are integral to their proper formation and function. We have identified the ε-tubulin gene in Tetrahymena thermophila and detected the protein, through fluorescence of a tagged allele, to basal bodies. Immunoelectron microscopy has shown that ε-tubulin localizes primarily to the core microtubule scaffold. A complete genomic knockout of ε-tubulin has revealed that it is an essential gene required for the assembly and maintenance of the triplet microtubule blades of basal bodies. We have conducted site-directed mutagenesis of the ε-tubulin gene and shown that residues within the nucleotide-binding domain, longitudinal interacting domains, and C-terminal tail are required for proper function. A single amino acid change of Thr150, a conserved residue in the nucleotide-binding domain, to Val is a conditional mutation that results in defects in the spatial and temporal assembly of basal bodies as well as their stability. We have genetically separated functions for the domains of ε-tubulin and identified a novel role for the nucleotide-binding domain in the regulation of basal body assembly and stability.

Indexed as

Basal BodiesCell CycleCentriolesCiliophora InfectionsMicrotubulesTetrahymena thermophilaTubulinTubulinBasal bodyEpsilon tubulinMicrotubule organizing centerTetrahymena thermophila

Identifiers

PMID23704354
PMCPMC3730247
OpenAlexW2120973691

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.