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Cited by 103Microtubule and mitosis dynamicsCancer Treatment and PharmacologyCellular Mechanics and Interactions

Acetylated Microtubules Are Preferentially Bundled Leading to Enhanced Kinesin-1 Motility

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Balabanian, Linda, Berger, Christopher L., Hendricks, Adam G.·2017·Biophysical Journal
DOI 10.1016/j.bpj.2017.08.009PMC PMC5627185
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Abstract

The motor proteins kinesin and dynein transport organelles, mRNA, proteins, and signaling molecules along the microtubule cytoskeleton. In addition to serving as tracks for transport, the microtubule cytoskeleton directs intracellular trafficking by regulating the activity of motor proteins through the organization of the filament network, microtubule-associated proteins, and tubulin posttranslational modifications. However, it is not well understood how these factors influence motor motility, and in vitro assays and live cell observations often produce disparate results. To systematically examine the factors that contribute to cytoskeleton-based regulation of motor protein motility, we extracted intact microtubule networks from cells and tracked the motility of single fluorescently labeled motor proteins on these cytoskeletons. We find that tubulin acetylation alone does not directly affect kinesin-1 motility. However, acetylated microtubules are predominantly bundled, and bundling enhances kinesin run lengths and provides a greater number of available kinesin binding sites. The neuronal MAP tau is also not sensitive to tubulin acetylation, but enriches preferentially on highly curved regions of microtubules where it strongly inhibits kinesin motility. Taken together, these results suggest that the organization of the microtubule network is a key contributor to the regulation of motor-based transport.

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  • In the remaining 6% of cells, exhibiting weak eGFP-tau expression, tau only localized to the microtubule bends.

    “In the remaining 6% of cells, exhibiting weak eGFP-tau expression, tau only localized to the microtubule bends, as described previously33,34.”

    From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [34]

    The section “Tau is enriched on curved microtubule segments” (page unavailable) reports preferential tau localization at bends in extracted cytoskeletal networks and notes that localization on curved microtubules has been observed in living cells. It does not report a 6% subgroup, weak eGFP-tau expression, or localization only at bends. (LLM, conf=0.88)

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Cited by

Sorted by citations

Authors
Balabanian, L., Berger, C. L., & Hendricks, A. G.
Affiliations
  • McGill University (CA)
  • University of Vermont (US)
Corresponding author
Hendricks, Adam G.
ORCID
Venue
Biophysical Journal
Publisher
Elsevier BV
Published
2017-10
Volume
113
Issue
7
Pages
1551-1560
ISSN
0006-3495 (ISSN-L)
DOI
10.1016/j.bpj.2017.08.009
PMC
PMC5627185
OpenAlex
W2762659278
Cited by
103
References
3
Citations by year
2026: 8 · 2025: 13 · 2024: 12 · 2023: 18 · 2022: 12 · 2021: 10 · 2020: 13 · 2019: 11 · 2018: 5 · 2017: 1
FWCI
4.27
Type
journal article
Language
en
Open access
Licence
Locations
  • Biophysical Journal (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Natural Sciences and Engineering Research Council of Canada (NSERC)
  • Fonds de Recherche du Québec – Nature et Technologies (FRQNT)
  • National Institutes of Health (NIH) (R01 GM101066)
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
kinesin-1, tubulin acetylation, microtubule bundling, microtubule curvature, motor protein motility, intracellular transport, microtubule cytoskeleton, tubulin post-translational modifications
MeSH terms
Acetylation, Animals, Chlorocebus aethiops, Escherichia coli, Microtubules, Recombinant Proteins, Tubulin, Kinesins, tau Proteins, COS Cells, Protein Transport, Rats

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