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PreprintCited by 25Microtubule and mitosis dynamicsCancer Treatment and PharmacologyCellular Mechanics and Interactions

Increased microtubule lattice spacing correlates with selective binding of kinesin-1 in cells

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de Jager, Leanne, Jansen, Klara I., Kapitein, Lukas C., Förster, Friedrich, Howes, Stuart C.·2022·The Journal of Cell Biology
DOI 10.1101/2022.05.25.493428PMC PMC11471893

Preprint — published as 10.1083/jcb.202206143 · Paper page

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Abstract

Within the cell cargo is transported via motor proteins walking along microtubules. The affinity of motor proteins for microtubules is controlled by various layers of regulation like tubulin isoforms, post- translational modifications and microtubule associated proteins. Recently, the conformation of the microtubule lattice has also emerged as a potential regulatory factor, but to what extent it acts as an additional layer of regulation has remained unclear. In this study, we used cryo-correlative light and electron microscopy to study microtubule lattices inside cells. We find that, while most microtubules have a compacted lattice (∼41 Å), a significant proportion of the microtubule cores have expanded lattice spacings and that these lattice spacings could be modulated by the microtubule stabilizing drug Taxol. Furthermore, kinesin-1 predominantly binds microtubules with a more expanded lattice spacing (∼41.6 Å). The different lattice spacings present in the cell can thus act as an additional factor that modulates the binding of motor proteins to specific microtubule subsets.

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  • Microtubules bound by StableMARK have an expanded lattice in cells, as indicated by fluorescence-guided cryo-focused ion beam transmission electron microscopy data.

    “Second, MTs bound by StableMARK have an expanded lattice in cells, as indicated by fluorescence-guided cryo-focused ion beam transmission electron microscopy data (de Jager et al., 2022 Preprint).”

    From A live-cell marker to visualize the dynamics of stable microtubules throughout the cell cycle (2023) · cites this paper as de Jager et al., 2022 Preprint

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Cited by

Sorted by citations

Authors
de Jager, L., Jansen, K. I., Kapitein, L. C., Förster, F., & Howes, S. C.
Affiliations
Utrecht University (NL)
Corresponding author
  • Kapitein, Lukas C.
  • Förster, Friedrich
  • Howes, Stuart C.
ORCID
Venue
The Journal of Cell Biology
Publisher
openRxiv
Published
2022-05-25
Volume
224
Issue
1
ISSN
0021-9525 (ISSN-L)
DOI
10.1101/2022.05.25.493428
PMC
PMC11471893
OpenAlex
W4403284162
Cited by
25
References
0
Citations by year
2026: 7 · 2025: 7 · 2024: 4 · 2023: 6 · 2022: 1
FWCI
4.03
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
Funders
  • Universiteit Utrecht
  • Radboud Universiteit
  • Nederlandse Organisatie voor Wetenschappelijk Onderzoek (022.006.001, 184.034.014, OCENW.XL21.XL21.048, 84.034.014)
  • Universitair Medisch Centrum Utrecht
  • European Research Council (724425, 819219)
  • H2020 European Research Council (724425)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords
microtubule lattice, lattice spacing, microtubule stability, paclitaxel, microtubule-associated proteins, microtubule dynamics, cryo-electron tomography
MeSH terms
Animals, Humans, Microtubule-Associated Proteins, Microtubules, Tubulin, Paclitaxel, Cryoelectron Microscopy, Electron Microscope Tomography

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