Evidence map›Paper›PMID 37086784›Full record

ArticleThe Journal of biological chemistry2023

Augmin is a Ran-regulated spindle assembly factor.

Jodi Kraus, Sophie M Travis, Matthew R King, Sabine Petry

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026
    Review
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  8. Review
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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

4 authors at 1 institution in 1 country.

Jodi KrausDepartment of Molecular Biology, Princeton University, Princeton, New Jersey, USA.
Sophie M TravisDepartment of Molecular Biology, Princeton University, Princeton, New Jersey, USA.
Matthew R KingDepartment of Molecular Biology, Princeton University, Princeton, New Jersey, USA.
Sabine PetryDepartment of Molecular Biology, Princeton University, Princeton, New Jersey, USA. Electronic address: spetry@princeton.edu.
Princeton University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Role and Mechanisms of Microtubule Nucleation in Spindle AssemblyR01GM141100 · NIGMS · PRINCETON UNIVERSITY · PI PETRY, SABINE · 2022 to 2025
$2.0M
Structure-based mechanism of the augmin complex in promoting branching microtubule nucleation and spindle assemblyF32GM142149 · NIGMS · PRINCETON UNIVERSITY · PI TRAVIS, SOPHIE M. · 2022 to 2023
$139k
NIGMS NIH HHS F32 GM142149NIGMS NIH HHS R01 GM141100NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

Mitotic spindles are composed of microtubules (MTs) that must nucleate at the right place and time. Ran regulates this process by directly controlling the release of spindle assembly factors (SAFs) from nucleocytoplasmic shuttle proteins importin-αβ and subsequently forms a biochemical gradient of SAFs localized around chromosomes. The majority of spindle MTs are generated by branching MT nucleation, which has been shown to require an eight-subunit protein complex known as augmin. In Xenopus laevis, Ran can control branching through a canonical SAF, TPX2, which is nonessential in Drosophila melanogaster embryos and HeLa cells. Thus, how Ran regulates branching MT nucleation when TPX2 is not required remains unknown. Here, we use in vitro pulldowns and total internal reflection fluorescence microscopy to show that augmin is a Ran-regulated SAF. We demonstrate that augmin directly interacts with both importin-α and importin-β through two nuclear localization sequences on the Haus8 subunit, which overlap with the MT-binding site. Moreover, we show that Ran controls localization of augmin to MTs in both Xenopus egg extract and in vitro. Our results demonstrate that RanGTP directly regulates augmin, which establishes a new way by which Ran controls branching MT nucleation and spindle assembly both in the absence and presence of TPX2.

Indexed as

Microtubule-Associated ProteinsMultiprotein Complexesran GTP-Binding ProteinXenopus Proteinsalpha KaryopherinsAnimalsbeta KaryopherinsCell Cycle ProteinsDrosophila melanogasterHeLa CellsHumansMicrotubule ProteinsMicrotubulesSpindle ApparatusXenopus laevisalpha Karyopherinsaugmin protein complex, Xenopusbeta KaryopherinsCell Cycle ProteinsMicrotubule-Associated ProteinsMicrotubule ProteinsMultiprotein Complexesran GTP-Binding ProteinTPX2 protein, XenopusXenopus Proteinsaugminbranching microtubule nucleationimportinsRan pathwayspindle assembly factorTPX2

Identifiers

PMID37086784
PMCPMC10318467
OpenAlexW4366606510

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.