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Cited by 89Microtubule and mitosis dynamicsGenetic and Kidney Cyst DiseasesCancer Treatment and Pharmacology

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

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Howes, Stuart C., Geyer, Elisabeth A., LaFrance, Benjamin, Zhang, Rui, Kellogg, Elizabeth H., Westermann, Stefan, Rice, Luke M., Nogales, Eva·2017·Journal of Cell Biology
DOI 10.1083/jcb.201612195PMC PMC5584162
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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.

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  • In non-mammalian species, microtubule lattice compaction does not appear to be directly coupled to GTP hydrolysis.

    “in non-mammalian species, microtubule lattice compaction does not appear to be directly coupled to GTP hydrolysis47,48.”

    From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [47]

    The Conclusions report that dynamic yeast microtubules did not show the compaction seen in mammalian microtubules, but say this might reflect either less GTP hydrolysis or a different conformational response. The paper therefore does not establish that compaction is uncoupled from hydrolysis, and its yeast findings do not cover non-mammalian species generally. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Authors
Howes, S. C., Geyer, E. A., LaFrance, B., Zhang, R., Kellogg, E. H., Westermann, S., Rice, L. M., & Nogales, E.
Affiliations
  • University of California, Berkeley (US)
  • The University of Texas Southwestern Medical Center (US)
  • Howard Hughes Medical Institute (US)
  • University of Duisburg-Essen (DE)
  • QB3 (US)
Corresponding author
Nogales, Eva
ORCID
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2017-06-26
Volume
216
Issue
9
Pages
2669-2677
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.201612195
PMC
PMC5584162
OpenAlex
W2673913370
Cited by
89
References
0
Citations by year
2026: 12 · 2025: 9 · 2024: 8 · 2023: 10 · 2022: 5 · 2021: 6 · 2020: 8 · 2019: 11 · 2018: 15 · 2017: 5
FWCI
5.56
Type
journal article
Language
en
Open access
Licence
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
  • National Science Foundation (1106400)
  • NSF (MCB 1054947, 1615938, 2014177758)
  • National Institutes of Health (R01-GM098543)
  • NIH (T32 GM008297, P01-GM051487)
  • Howard Hughes Medical Institute
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
  • Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
Keywords
microtubules, tubulin, GTP hydrolysis, Bim1, plus-end tracking proteins, microtubule disassembly, polymerization dynamics, allosteric communication, cryo-electron microscopy
MeSH terms
Animals, Binding Sites, Guanosine Triphosphate, Hydrolysis, Microtubule Proteins, Microtubules, Protein Binding, Saccharomyces cerevisiae, Structure-Activity Relationship, Tubulin, Cell Cycle Proteins, Cryoelectron Microscopy, Protein Structure, Quaternary, Saccharomyces cerevisiae Proteins, Sus scrofa, Protein Multimerization, Molecular Dynamics Simulation

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