Evidence map›Paper›PMID 28652389›Full record

ArticleThe Journal of cell biology2017

Structural differences between yeast and mammalian microtubules revealed by cryo-EM.

Stuart C Howes, Elisabeth A Geyer, Benjamin LaFrance, Rui Zhang, Elizabeth H Kellogg, Stefan Westermann, Luke M Rice, Eva Nogales

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
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  7. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    Review
  8. Article
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  14. Physiological roles of chloride ions in bodily and cellular functions.The journal of physiological sciences : JPS · 2023
    Review
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  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

8 authors at 5 institutions in 2 countries.

Stuart C HowesBiophysics Graduate Group, University of California, Berkeley, Berkeley, CA.ORCID 0000-0001-6129-1882
Elisabeth A GeyerDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX.
Benjamin LaFranceMolecular and Cell Biology Graduate Program, University of California, Berkeley, Berkeley, CA.
Rui ZhangHoward Hughes Medical Institute, University of California, Berkeley, Berkeley, CA.
Elizabeth H KelloggHoward Hughes Medical Institute, University of California, Berkeley, Berkeley, CA.
Stefan WestermannDepartment of Molecular Genetics, Center for Medical Biotechnology, University of Duisburg-Essen, Essen, Germany.ORCID 0000-0001-6921-9113
Luke M RiceDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX.
Eva NogalesHoward Hughes Medical Institute, University of California, Berkeley, Berkeley, CA enogales@lbl.gov.ORCID 0000-0001-9816-3681
Howard Hughes Medical Institute · USThe University of Texas Southwestern Medical Center · USUniversity of California, Berkeley · USQB3 · USUniversity of Duisburg-Essen · DE

Funding

THE MOLECULAR BASIS OF CELL FUNCTIONT32GM007232 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BILDER, DAVID, UNAL, ELCIN · 1985 to 2022
$36.4M
TUBULIN STRUCTURE BY ELECTRON CRYSTALLOGRAPHYP01GM051487 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CATE, JAMIE H · 1994 to 2018
$27.6M
CONFORMATION & RECOGNITION IN MICROTUBLE DYNAMICSR01GM098543 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RICE, LUKE W · 2011 to 2023
$4.2M
Molecular Biophysics Predoctoral Training ProgramT32GM008297 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 1989 to 2018
$2.4M
Howard Hughes Medical InstituteNIGMS NIH HHS P01 GM051487NIGMS NIH HHS R01 GM098543NIGMS NIH HHS T32 GM007232NIGMS NIH HHS T32 GM008297
6 · The paper itself

Abstract

Microtubules are polymers of αβ-tubulin heterodimers essential for all eukaryotes. Despite sequence conservation, there are significant structural differences between microtubules assembled in vitro from mammalian or budding yeast tubulin. Yeast MTs were not observed to undergo compaction at the interdimer interface as seen for mammalian microtubules upon GTP hydrolysis. Lack of compaction might reflect slower GTP hydrolysis or a different degree of allosteric coupling in the lattice. The microtubule plus end-tracking protein Bim1 binds yeast microtubules both between αβ-tubulin heterodimers, as seen for other organisms, and within tubulin dimers, but binds mammalian tubulin only at interdimer contacts. At the concentrations used in cryo-electron microscopy, Bim1 causes the compaction of yeast microtubules and induces their rapid disassembly. Our studies demonstrate structural differences between yeast and mammalian microtubules that likely underlie their differing polymerization dynamics. These differences may reflect adaptations to the demands of different cell size or range of physiological growth temperatures.

Indexed as

Cryoelectron MicroscopyAnimalsBinding SitesCell Cycle ProteinsGuanosine TriphosphateHydrolysisMicrotubule ProteinsMicrotubulesMolecular Dynamics SimulationProtein BindingProtein MultimerizationProtein Structure, QuaternarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipSus scrofaBIM1 protein, S cerevisiaeCell Cycle ProteinsGuanosine TriphosphateMicrotubule ProteinsSaccharomyces cerevisiae ProteinsTubulin

Identifiers

PMID28652389
PMCPMC5584162
OpenAlexW2673913370

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.