Evidence map›Paper›PMID 17978090›Full record

ArticleMolecular biology of the cell2008

The structure of the gamma-tubulin small complex: implications of its architecture and flexibility for microtubule nucleation.

Justin M Kollman, Alex Zelter, Eric G D Muller, Bethany Fox, Luke M Rice, Trisha N Davis, David A Agard

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

59 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure of the γ-tubulin ring complex-capped microtubule.Nature structural & molecular biology · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. FRET Microscopy in Yeast.Biosensors · 2019
    Review
  18. Article
  19. Article
  20. Review
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

7 authors at 2 institutions in 1 country.

Justin M KollmanDepartment of Biochemistry and Biophysics and the Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158, USA.
Alex Zelter
Eric G D Muller
Bethany Fox
Luke M Rice
Trisha N Davis
David A Agard
University of Washington · USHoward Hughes Medical Institute · US

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
MOLECULAR ANALYSIS OF THE SPINDLE POLE BODYR01GM040506 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAVIS, TRISHA N. · 1988 to 2018
$8.6M
Microtubule Nucleation: Structure & MechanismR01GM031627 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AGARD, DAVID A. · 1985 to 2016
$6.1M
The Structural Basis of Microtubule Nucleation by gamma-TuSCF32GM078790 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KOLLMAN, JUSTIN M · 2006 to 2008
$120k
Howard Hughes Medical InstituteNCRR NIH HHS P41 RR-011823NCRR NIH HHS P41 RR011823NIGMS NIH HHS F32 GM-078790NIGMS NIH HHS F32 GM078790NIGMS NIH HHS R01 GM031627NIGMS NIH HHS R01 GM-040506NIGMS NIH HHS R01 GM040506NIGMS NIH HHS R01 GM-31627
6 · The paper itself

Abstract

The gamma-tubulin small complex (gamma-TuSC) is an evolutionarily conserved heterotetramer essential for microtubule nucleation. We have determined the structure of the Saccharomyces cerevisiae gamma-TuSC at 25-A resolution by electron microscopy. gamma-TuSC is Y-shaped, with an elongated body connected to two arms. Gold labeling showed that the two gamma-tubulins are located in lobes at the ends of the arms, and the relative orientations of the other gamma-TuSC components were determined by in vivo FRET. The structures of different subpopulations of gamma-TuSC indicate flexibility in the connection between a mobile arm and the rest of the complex, resulting in variation of the relative positions and orientations of the gamma-tubulins. In all of the structures, the gamma-tubulins are distinctly separated, a configuration incompatible with the microtubule lattice. The separation of the gamma-tubulins in isolated gamma-TuSC likely plays a role in suppressing its intrinsic microtubule-nucleating activity, which is relatively weak until the gamma-TuSC is incorporated into higher order complexes or localized to microtubule-organizing centers. We propose that further movement of the mobile arm is required to bring the gamma-tubulins together in microtubule-like interactions, and provide a template for microtubule growth.

Indexed as

Fluorescence Resonance Energy TransferMicroscopy, ElectronMicrotubulesModels, MolecularNucleotidesPliabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTubulinNucleotidesSaccharomyces cerevisiae ProteinsTUB4 protein, S cerevisiaeTubulin

Identifiers

PMID17978090
PMCPMC2174199
OpenAlexW2104753069

What OpenQuestion holds

Textmetadata
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.