Evidence map›Paper›PMID 29695792›Full record

ArticleNature cell biology2018

XMAP215 is a microtubule nucleation factor that functions synergistically with the γ-tubulin ring complex.

Akanksha Thawani, Rachel S Kadzik, Sabine Petry

Abstract readVideo-Audio Media
In one paragraph

Article in Nature cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing 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

100 citing papers in PubMed, 178 citations in OpenAlex.

  1. Article
  2. Article
  3. The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026
    Review
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  17. Structure of the γ-tubulin ring complex-capped microtubule.Nature structural & molecular biology · 2024
    Article
  18. Article
  19. Article
  20. Article

40 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Akanksha ThawaniDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA.
Rachel S KadzikDepartment of Molecular Biology, Princeton University, Princeton, NJ, USA.
Sabine PetryDepartment of Molecular Biology, Princeton University, Princeton, NJ, USA. spetry@princeton.edu.ORCID http://orcid.org/0000-0002-8537-9763
Princeton University · US

Funding

Building the Chromosome Segregation Machinery from ScratchDP2GM123493 · NIGMS · PRINCETON UNIVERSITY · PI PETRY, SABINE · 2016 to 2016
$2.4M
Determining the molecular mechanism of localizing and activating the gamma-tubulin ring complex (gamma-TuRC) at the centrosomeF32GM119195 · NIGMS · PRINCETON UNIVERSITY · PI KADZIK, RACHEL S · 2016 to 2017
$103k
NIGMS NIH HHS DP2 GM123493NIGMS NIH HHS F32 GM119195
6 · The paper itself

Abstract

How microtubules (MTs) are generated in the cell is a major question in understanding how the cytoskeleton is assembled. For several decades, γ-tubulin has been accepted as the universal MT nucleator of the cell. Although there is evidence that γ-tubulin complexes are not the sole MT nucleators, identification of other nucleation factors has proven difficult. Here, we report that the well-characterized MT polymerase XMAP215 (chTOG/Msps/Stu2p/Alp14/Dis1 homologue) is essential for MT nucleation in Xenopus egg extracts. The concentration of XMAP215 determines the extent of MT nucleation. Even though XMAP215 and the γ-tubulin ring complex (γ-TuRC) possess minimal nucleation activity individually, together, these factors synergistically stimulate MT nucleation in vitro. The amino-terminal TOG domains 1-5 of XMAP215 bind to αβ-tubulin and promote MT polymerization, whereas the conserved carboxy terminus is required for efficient MT nucleation and directly binds to γ-tubulin. In summary, XMAP215 and γ-TuRC together function as the principal nucleation module that generates MTs in cells.

Indexed as

AnimalsMicrotubule-Associated ProteinsMicrotubule-Organizing CenterMicrotubulesMultiprotein ComplexesProtein BindingProtein Interaction Domains and MotifsSignal TransductionTime FactorsTubulinXenopus laevisXenopus ProteinsCKAP5 protein, XenopusMicrotubule-Associated ProteinsMultiprotein ComplexesTubulinXenopus Proteins

Identifiers

PMID29695792
PMCPMC5926803
OpenAlexW2802035309

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.