Evidence map›Paper›PMID 38609661›Full record

ArticleNature structural & molecular biology2024

Structure of the γ-tubulin ring complex-capped microtubule.

Amol Aher, Linas Urnavicius, Allen Xue, Kasahun Neselu, Tarun M Kapoor

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
12.1field-weighted citation impact, top 1% 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

23 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026
    Review
  7. Article
  8. Review
  9. Article
  10. Microtubule Minus-End Binding Proteins in Cancer: Advances.Diagnostics (Basel, Switzerland) · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. ProSComputational and structural biotechnology journal · 2025
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Amol Aher *Laboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY, USA.
Linas Urnavicius *Laboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY, USA.
Allen XueLaboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY, USA.
Kasahun NeseluSimons Electron Microscopy Center, New York Structural Biology Center, New York, NY, USA.
Tarun M KapoorLaboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY, USA. kapoor@rockefeller.edu.ORCID http://orcid.org/0000-0003-0628-211X
Rockefeller University · USNew York Structural Biology Center · US

Funding

Chemical Biology of Cell Division - Revision - 2R35GM130234 · NIGMS · ROCKEFELLER UNIVERSITY · PI TARUN M. KAPOOR · 2019 to 2026
$6.0M
NIGMS NIH HHS R35 GM130234
6 · The paper itself

Abstract

Microtubules are composed of α-tubulin and β-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules assemble with the canonical 13-protofilament architecture, resulting in micrometer-scale α/β-tubulin tracks for intracellular transport that align with, rather than spiral along, the long axis of the filament. We report that the human ~2.3 MDa γ-tubulin ring complex (γ-TuRC), an essential regulator of microtubule formation that contains 14 γ-tubulins, selectively nucleates 13-protofilament microtubules. Cryogenic electron microscopy reconstructions of γ-TuRC-capped microtubule minus ends reveal the extensive intra-domain and inter-domain motions of γ-TuRC subunits that accommodate luminal bridge components and establish lateral and longitudinal interactions between γ-tubulins and α-tubulins. Our structures suggest that γ-TuRC, an inefficient nucleation template owing to its splayed conformation, can transform into a compacted cap at the microtubule minus end and set the lattice architecture of cellular microtubules.

Indexed as

Cryoelectron MicroscopyMicrotubulesModels, MolecularTubulinHumansMicrotubule-Associated ProteinsProtein ConformationMicrotubule-Associated ProteinsTubulin

Identifiers

PMID38609661
PMCPMC11257807
OpenAlexW4394753118

What OpenQuestion holds

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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.