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Cited by 83Microtubule and mitosis dynamicsProtein Structure and DynamicsGenetic and Kidney Cyst Diseases

The evolution of the structure of tubulin and its potential consequences for the role and function of microtubules in cells and embryos

Tuszynski, Jack A., Carpenter, Eric J., Huzil, J T., Malinski, Wojtek, Luchko, Tyler, Luduena, Richard F.·2006·The International Journal of Developmental Biology
DOI 10.1387/ijdb.052063jt
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Abstract

This paper discusses the results of homology modeling and resulting calculation of key structural and physical properties for close to 300 tubulin sequences, including alpha, beta, gamma, delta and epsilon -tubulins. The basis for our calculations was the structure of the tubulin dimer published several years ago by Nogales et al. (1998), later refined to 3.5 resolution by Lowe et al. (2001). While, it appears that the alpha, beta and gamma-tubulins segregate into distinct structural families, we have found several differences in the physical properties within each group. Each of the alpha, beta and gamma- tubulin groups exhibit major differences in their net electric charge, dipole moments and dipole vector orientations. These properties could influence functional characteristics such as microtubule stability and assembly kinetics, due to their effects on the strength of protein-protein interactions. In addition to the general structural trends between tubulin isoforms, we have observed that the carboxy-termini of alpha and beta-tubulin exists in at least two stable configurations, either projecting away from the tubulin (or microtubule) surface, or collapsed onto the surface. In the latter case, the carboxy-termini form a lattice distinctly different from that of the well-known A and B lattices formed by the tubulin subunits. However, this C-terminal lattice is indistinguishable from the lattice formed when the microtubule-associated protein tau binds to the microtubule surface. Finally, we have discussed how tubulin sequence diversity arose in evolution giving rise to its particular phylogeny and how it may be used in cell- and tissue-specific expression including embryonal development.

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  • The almost perfect radial symmetry of tubulin dipole arrangements in an MT has been predicted by a computer simulation.

    “this is very unlikely because of the almost perfect radial symmetry of tubulin dipole arrangements in an MT, which has been predicted by a computer simulation [70].”

    From An Overview of Sub-Cellular Mechanisms Involved in the Action of TTFields (2016) · cites this paper as [70]

  • The dipole moment is strongly tubulin-isotype dependent, varying from 500 to 4000 debye between various tubulin isotypes.

    “this is also strongly tubulin-isotype dependent, so these numbers vary a lot between various tubulin isotypes from 500 to 4000 debye [70].”

    From An Overview of Sub-Cellular Mechanisms Involved in the Action of TTFields (2016) · cites this paper as [70]

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Authors
Tuszynski, J. A., Carpenter, E. J., Huzil, J. T., Malinski, W., Luchko, T., & Luduena, R. F.
Affiliations
University of Alberta (CA)
ORCID
Venue
The International Journal of Developmental Biology
Publisher
EHU Press
Published
2006
Volume
50
Issue
2-3
Pages
341-358
ISSN
0214-6282 (ISSN-L)
DOI
10.1387/ijdb.052063jt
OpenAlex
W2016262807
Cited by
83
References
67
Citations by year
2026: 4 · 2025: 2 · 2024: 4 · 2023: 1 · 2022: 5 · 2021: 4 · 2020: 5 · 2019: 9 · 2018: 1 · 2017: 3 · 2016: 2 · 2015: 2 · 2014: 8 · 2013: 4 · 2012: 5
FWCI
2.35
Type
journal article
Language
en
Open access
closed
Locations
  • The International Journal of Developmental Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Cancer Institute (P30CA 54174, P30CA054174)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
Keywords
tubulin, microtubules, tubulin isoforms, homology modeling, electric charge, dipole moment, tau protein, microtubule stability, protein-protein interaction, embryonic development, tissue-specific gene expression
MeSH terms
Amino Acid Sequence, Animals, Binding Sites, Cell Physiological Phenomena, Cells, Humans, Microtubules, Models, Biological, Molecular Sequence Data, Tubulin, Protein Structure, Tertiary, Evolution, Molecular, Dimerization, Embryonic Development, Static Electricity

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