Evidence map›Paper›PMID 28900268›Full record

ArticleScientific reports2017

Interrogation of γ-tubulin alleles using high-resolution fitness measurements reveals a distinct cytoplasmic function in spindle alignment.

Kristian Shulist, Eric Yen, Susanne Kaitna, Allen Leary, Alexandra Decterov, Debarun Gupta, Jackie Vogel

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

5 citing papers in PubMed, 16 citations in OpenAlex.

  1. γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Kristian ShulistDepartment of Biology, McGill University, 3649 Promenade Sir William Osler, Montreal, Quebec, H3G 0B1, Canada.
Eric YenDepartment of Biology, McGill University, 3649 Promenade Sir William Osler, Montreal, Quebec, H3G 0B1, Canada.
Susanne KaitnaDepartment of Biology, McGill University, 3649 Promenade Sir William Osler, Montreal, Quebec, H3G 0B1, Canada.
Allen LearyDepartment of Biology, McGill University, 3649 Promenade Sir William Osler, Montreal, Quebec, H3G 0B1, Canada.
Alexandra DecterovDepartment of Biology, McGill University, 3649 Promenade Sir William Osler, Montreal, Quebec, H3G 0B1, Canada.
Debarun GuptaDepartment of Biology, McGill University, 3649 Promenade Sir William Osler, Montreal, Quebec, H3G 0B1, Canada.
Jackie VogelDepartment of Biology, McGill University, 3649 Promenade Sir William Osler, Montreal, Quebec, H3G 0B1, Canada. jackie.vogel@mcgill.ca.
McGill University · CA

Funding

CIHR 123335
6 · The paper itself

Abstract

γ-Tubulin has a well-established role in nucleating the assembly of microtubules, yet how phosphorylation regulates its activity remains unclear. Here, we use a time-resolved, fitness-based SGA approach to compare two γ-tubulin alleles, and find that the genetic interaction profile of γtub-Y362E is enriched in spindle positioning and cell polarity genes relative to that of γtub-Y445D, which is enriched in genes involved in spindle assembly and stability. In γtub-Y362E cells, we find a defect in spindle alignment and an increase in the number of astral microtubules at both spindle poles. Our results suggest that the γtub-Y362E allele is a separation-of-function mutation that reveals a role for γ-tubulin phospho-regulation in spindle alignment. We propose that phosphorylation of the evolutionarily conserved Y362 residue of budding yeast γ-tubulin contributes to regulating the number of astral microtubules associated with spindle poles, and promoting efficient pre-anaphase spindle alignment.

Indexed as

AllelesCell LineCell PolarityDyneinsMicrotubulesMutationNuclear ProteinsPhosphorylationSaccharomyces cerevisiae ProteinsSaccharomycetalesSignal TransductionSpindle Pole BodiesTubulinDyneinsKAR9 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae ProteinsTubulin

Identifiers

PMID28900268
PMCPMC5595808
OpenAlexW2751646908

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.