Evidence map›Paper›PMID 26224545›Full record

ArticleMolecular microbiology2015

γ-Tubulin complex in Trypanosoma brucei: molecular composition, subunit interdependence and requirement for axonemal central pair protein assembly.

Qing Zhou, Ziyin Li

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. TheCells · 2021
    Review
  7. Review
  8. Alpha-Tubulin Acetylation inFrontiers in cellular and infection microbiology · 2021
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. The Central Apparatus of Cilia and Eukaryotic Flagella.Cold Spring Harbor perspectives in biology · 2017
    Review
  17. 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

2 authors at 1 institution in 1 country.

Qing ZhouDepartment of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas, 77030, USA.
Ziyin LiDepartment of Microbiology and Molecular Genetics, University of Texas Medical School at Houston, Houston, Texas, 77030, USA.
The University of Texas Health Science Center at Houston · US

Funding

Mechanisms Of The Unusual Cytokinesis In TrypanosomesR01AI101437 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LI, ZIYIN · 2013 to 2025
$6.4M
Regulation of cell cycle transitions by CRK1 and CRK3 in trypanosomesR56AI108657 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LI, ZIYIN · 2015 to 2015
$383k
NIAID NIH HHS AI101437NIAID NIH HHS AI108657NIAID NIH HHS R01 AI101437NIAID NIH HHS R56 AI108657
6 · The paper itself

Abstract

γ-Tubulin complex constitutes a key component of the microtubule-organizing center and nucleates microtubule assembly. This complex differs in complexity in different organisms: the budding yeast contains the γ-tubulin small complex (γTuSC) composed of γ-tubulin, gamma-tubulin complex protein (GCP)2 and GCP3, whereas animals contain the γ-tubulin ring complex (γTuRC) composed of γTuSC and three additional proteins, GCP4, GCP5 and GCP6. In Trypanosoma brucei, the composition of the γ-tubulin complex remains elusive, and it is not known whether it also regulates assembly of the subpellicular microtubules and the spindle microtubules. Here we report that the γ-tubulin complex in T. brucei is composed of γ-tubulin and three GCP proteins, GCP2-GCP4, and is primarily localized in the basal body throughout the cell cycle. Depletion of GCP2 and GCP3, but not GCP4, disrupted the axonemal central pair microtubules, but not the subpellicular microtubules and the spindle microtubules. Furthermore, we showed that the γTuSC is required for assembly of two central pair proteins and that γTuSC subunits are mutually required for stability. Together, these results identified an unusual γ-tubulin complex in T. brucei, uncovered an essential role of γTuSC in central pair protein assembly, and demonstrated the interdependence of individual γTuSC components for maintaining a stable complex.

Indexed as

AnimalsAxonemeCell CycleFlagellaMicrotubule-Associated ProteinsMicrotubule-Organizing CenterProtein BindingProtozoan ProteinsTrypanosoma brucei bruceiTubulinMicrotubule-Associated ProteinsProtozoan ProteinsTubulin

Identifiers

PMID26224545
PMCPMC4636443
OpenAlexW2106160709

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Registered trials

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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.