Transitions in microtubule C-termini conformations as a possible dendritic signaling phenomenon
Open accessAbstract
We model the dynamical states of the C-termini of tubulin dimers that comprise neuronal microtubules. We use molecular dynamics and other computational tools to explore the time-dependent behavior of conformational states of a C-terminus of tubulin within a microtubule and assume that each C-terminus interacts via screened Coulomb forces with the surface of a tubulin dimer, with neighboring C-termini and also with any adjacent microtubule-associated protein 2 (MAP2). Each C-terminus can either bind to the tubulin surface via one of the several positively charged regions or can be allowed to explore the space available in the solution surrounding the dimer. We find that the preferential orientation of each C-terminus is away from the tubulin surface but binding to the surface may also take place, albeit at a lower probability. The results of our model suggest that perturbations generated by the C-termini interactions with counterions surrounding a MAP2 may propagate over distances greater than those between adjacent microtubules. Thus, the MAP2 structure is able to act as a kind of biological wire (or a cable) transmitting local electrostatic perturbations resulting in ionic concentration gradients from one microtubule to another. We briefly discuss the implications the current dynamic modeling may have on synaptic activation and potentiation.
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This wave is predicted to travel as a 'kink' solitary wave with a phase velocity of vph = 2 nm/ps.
“This wave is predicted to travel as a “kink” solitary wave with a phase velocity of vph = 2 nm/ps [97].”
From An Overview of Sub-Cellular Mechanisms Involved in the Action of TTFields (2016) · cites this paper as [97]
Computer simulations demonstrate that ionic waves can trigger C-termini to change from upright to downward conformations initiating propagation of a travelling wave.
“Computer simulations demonstrate that ionic waves can trigger C-termini to change from upright to downward conformations initiating propagation of a travelling wave [97].”
From An Overview of Sub-Cellular Mechanisms Involved in the Action of TTFields (2016) · cites this paper as [97]
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- Authors
- Priel, A., Tuszynski, J. A., & Woolf, N. J.
- Affiliations
- University of Alberta (CA)
- University of California, Los Angeles (US)
- ORCID
- Priel, Avner
- Venue
- European Biophysics Journal
- Published
- 2005-09-24
- Volume
- 35
- Issue
- 1
- Pages
- 40-52
- ISSN
- 0175-7571 (ISSN-L)
- 1432-1017
- OpenAlex
- W2003477962
- Cited by
- 57
- References
- 27
- Citations by year
- 2025: 3 · 2024: 2 · 2023: 1 · 2021: 1 · 2020: 5 · 2019: 3 · 2018: 2 · 2016: 2 · 2014: 6 · 2013: 2 · 2012: 4
- FWCI
- 0.82
- Type
- journal article
- Language
- en
- Open access
- green
- arxiv.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- European Biophysics Journal (publishedVersion)
- PubMed (publishedVersion)
- arXiv (Cornell University) (submittedVersion)
- arXiv (Cornell University)
- Funders
- National Institutes of Health
- Natural Sciences and Engineering Research Council of Canada
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Electrostatics and Colloid Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- tubulin dimers, MAP2, dendritic signaling, electrostatic interactions, Coulomb screening, ion gradients, microtubule dynamics, synaptic potentiation, neuronal microtubules
- MeSH terms
- Dendrites, Humans, Microtubule-Associated Proteins, Microtubules, Molecular Conformation, Protein Binding, Species Specificity, Time Factors, Tubulin, Signal Transduction, Dimerization, Static Electricity
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