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Cited by 37Microtubule and mitosis dynamicsCancer Treatment and PharmacologyGenetic and Kidney Cyst Diseases

Causes, costs and consequences of kinesin motors communicating through the microtubule lattice

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Verhey, Kristen J., Ohi, Ryoma·2023·Journal of Cell Science
DOI 10.1242/jcs.260735PMC PMC10022682
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Abstract

Microtubules are critical for a variety of important functions in eukaryotic cells. During intracellular trafficking, molecular motor proteins of the kinesin superfamily drive the transport of cellular cargoes by stepping processively along the microtubule surface. Traditionally, the microtubule has been viewed as simply a track for kinesin motility. New work is challenging this classic view by showing that kinesin-1 and kinesin-4 proteins can induce conformational changes in tubulin subunits while they are stepping. These conformational changes appear to propagate along the microtubule such that the kinesins can work allosterically through the lattice to influence other proteins on the same track. Thus, the microtubule is a plastic medium through which motors and other microtubule-associated proteins (MAPs) can communicate. Furthermore, stepping kinesin-1 can damage the microtubule lattice. Damage can be repaired by the incorporation of new tubulin subunits, but too much damage leads to microtubule breakage and disassembly. Thus, the addition and loss of tubulin subunits are not restricted to the ends of the microtubule filament but rather, the lattice itself undergoes continuous repair and remodeling. This work leads to a new understanding of how kinesin motors and their microtubule tracks engage in allosteric interactions that are critical for normal cell physiology.

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  • Lattice conformation is emerging as an important, understudied constituent of the 'tubulin code'.

    “Next to microtubule post-translational modifications and tubulin isotypes, lattice conformation is emerging as an important, understudied constituent of the 'tubulin code', the structural, biochemical and functional diversification of microtubule subsets in the same cell 68-70 .”

    From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [69]

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Authors
Verhey, K. J., & Ohi, R.
Affiliations
University of Michigan (US)
Corresponding author
Ohi, Ryoma
ORCID
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
2023-03-01
Volume
136
Issue
5
ISSN
  • 0021-9533 (ISSN-L)
  • 1477-9137
DOI
10.1242/jcs.260735
PMC
PMC10022682
OpenAlex
W4323037554
Cited by
37
References
113
Citations by year
2026: 10 · 2025: 15 · 2024: 9 · 2023: 3
FWCI
5.33
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Cell Science (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (R35GM131744, R01GM086610)
  • University of Michigan
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 › Genetics › Genetic and Kidney Cyst Diseases
Keywords
kinesin motors, microtubule lattice, kinesin-1, kinesin-4, allosteric communication, microtubule-associated proteins, microtubule disassembly, intracellular cargo transport, microtubule remodeling
MeSH terms
Cytoskeleton, Microtubule-Associated Proteins, Microtubules, Tubulin, Kinesins

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