Evidence map›Paper›PMID 27226487›Full record

ArticleMolecular biology of the cell2016

Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly.

Andrew S Lyon, Geneviève Morin, Michelle Moritz, King Clyde B Yabut, Tamira Vojnar, Alex Zelter, Eric Muller, Trisha N Davis, David A Agard

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

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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

9 authors at 2 institutions in 1 country.

Andrew S LyonDepartment of Biochemistry and Biophysics and Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158.
Geneviève MorinDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Michelle MoritzDepartment of Biochemistry and Biophysics and Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158.
King Clyde B YabutDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Tamira VojnarDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Alex ZelterDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Eric MullerDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Trisha N DavisDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
David A AgardDepartment of Biochemistry and Biophysics and Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158 agard@msg.ucsf.edu.
University of Washington · USHoward Hughes Medical Institute · US

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
The Yeast Centrosome - Structure Assembly & FunctionP01GM105537 · NIGMS · UNIVERSITY OF COLORADO · PI WINEY, MARK · 2014 to 2018
$8.3M
Microtubule Nucleation: Structure & MechanismR01GM031627 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AGARD, DAVID A. · 1985 to 2016
$6.1M
Structure & Mechanism: microtubule nucleation, centrosomes, phage cytoskeletonR35GM118099 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AGARD, DAVID A. · 2016 to 2022
$3.6M
Howard Hughes Medical InstituteNIGMS NIH HHS P01 GM105537NIGMS NIH HHS P41 GM103533NIGMS NIH HHS R01 GM031627NIGMS NIH HHS R35 GM118099
6 · The paper itself

Abstract

The microtubule (MT) cytoskeleton plays important roles in many cellular processes. In vivo, MT nucleation is controlled by the γ-tubulin ring complex (γTuRC), a 2.1-MDa complex composed of γ-tubulin small complex (γTuSC) subunits. The mechanisms underlying the assembly of γTuRC are largely unknown. In yeast, the conserved protein Spc110p both stimulates the assembly of the γTuRC and anchors the γTuRC to the spindle pole body. Using a quantitative in vitro FRET assay, we show that γTuRC assembly is critically dependent on the oligomerization state of Spc110p, with higher-order oligomers dramatically enhancing the stability of assembled γTuRCs. Our in vitro findings were confirmed with a novel in vivo γTuSC recruitment assay. We conclude that precise spatial control over MT nucleation is achieved by coupling localization and higher-order oligomerization of the receptor for γTuRC.

Indexed as

Amino Acid SequenceCalmodulin-Binding ProteinsCentrosomeCytoskeletal ProteinsMicrotubule-Associated ProteinsMicrotubule-Organizing CenterMicrotubulesNuclear ProteinsProtein BindingProtein Structure, QuaternaryProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusTubulinCalmodulin-Binding ProteinsCytoskeletal ProteinsMicrotubule-Associated ProteinsNuclear ProteinsProtein SubunitsSaccharomyces cerevisiae ProteinsSPC110 protein, S cerevisiaeTubulin

Identifiers

PMID27226487
PMCPMC4945142
OpenAlexW2395003376

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.