dorsal/arxiv
View SchemaTransitions in Microtubule C-termini conformations as a possible Dendritic signaling phenomenon
| Authors | Avner Priel, Jack A. Tuszynski, Nancy J. Woolf |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0506024 |
| URL | https://arxiv.org/abs/q-bio/0506024 |
| DOI | 10.1007/s00249-005-0003-0 |
| Journal | European Biophysics Journal 35(1):40-52 (2005) |
Abstract
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 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 counter-ions 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 implications the current dynamic modeling may have on synaptic activation and potentiation.
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"abstract": "We model the dynamical states of the C-termini of tubulin dimers that\ncomprise neuronal microtubules. We use molecular dynamics and other\ncomputational tools to explore the time-dependent behavior of conformational\nstates of a C-terminus of tubulin within a microtubule and assume that each\nC-terminus interacts via screened Coulomb forces with the surface of a tubulin\ndimer, with neighboring C-termini and also with any adjacent\nmicrotubule-associated protein 2 (MAP2). Each C-terminus can either bind to the\ntubulin surface via one of several positively charged regions or can be allowed\nto explore the space available in the solution surrounding the dimer. We find\nthat the preferential orientation of each C-terminus is away from the tubulin\nsurface but binding to the surface may also take place, albeit at a lower\nprobability. The results of our model suggest that perturbations generated by\nthe C-termini interactions with counter-ions surrounding a MAP2 may propagate\nover distances greater than those between adjacent microtubules. Thus, the MAP2\nstructure is able to act as a kind of biological wire (or a cable) transmitting\nlocal electrostatic perturbations resulting in ionic concentration gradients\nfrom one microtubule to another. We briefly discuss implications the current\ndynamic modeling may have on synaptic activation and potentiation.",
"arxiv_id": "q-bio/0506024",
"authors": [
"Avner Priel",
"Jack A. Tuszynski",
"Nancy J. Woolf"
],
"categories": [
"q-bio.SC",
"physics.bio-ph",
"physics.comp-ph",
"q-bio.NC"
],
"doi": "10.1007/s00249-005-0003-0",
"journal_ref": "European Biophysics Journal 35(1):40-52 (2005)",
"title": "Transitions in Microtubule C-termini conformations as a possible Dendritic signaling phenomenon",
"url": "https://arxiv.org/abs/q-bio/0506024"
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