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Microtubules01:35

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There are three types of cytoskeletal structures in eukaryotic cells—microfilaments, intermediate filaments, and microtubules. With a diameter of about 25 nm, microtubules are the thickest of these fibers. Microtubules carry out a variety of functions that include cell structure and support, transport of organelles, cell motility (movement), and the separation of chromosomes during cell division.
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Microtubules are the thickest cytoskeletal filaments with a diameter of 25 nm. In prokaryotic organisms, microtubules are commonly found in locomotory appendages like cilia and flagella. In eukaryotic cells, microtubules form specialized extensions for moving fluid over the surface, like those found in cells lining the intestine.
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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
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Microtubules are dynamic structures that undergo continuous assembly and disassembly. They originate from specialized multi-protein complexes known as microtubule organizing centers or MTOCs. Within the MTOC, the point of origin of the microtubule is known as the minus end, while the end radiating outward is the plus end. Microtubules serve two primary functions — the organization of spindle complexes to separate sister chromatids during mitotic or meiotic cell division and the formation...
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Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
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Catastrophic depolymerization of microtubules driven by subunit shape change.

Jonathan A Bollinger1, Mark J Stevens

  • 1Center for Integrated Nanotechnologies, Sandia National Laboratories, Albuquerque NM 87185, USA. msteve@sandia.gov.

Soft Matter
|January 26, 2018
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Summary
This summary is machine-generated.

Microtubule depolymerization is driven by GTP-tubulin dephosphorylation causing shape changes. This shape alteration destabilizes microtubules, leading to depolymerization, unless stabilized by GTP-tubulin caps.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Dynamics

Background:

  • Microtubules are essential cytoskeletal polymers exhibiting dynamic instability.
  • This instability involves cycles of polymerization (growth) and depolymerization (catastrophe).
  • GTP-tubulin self-assembles, but GTP hydrolysis to GDP within the microtubule destabilizes it.

Purpose of the Study:

  • To investigate the mechanical basis of microtubule destabilization.
  • To test the hypothesis that tubulin dephosphorylation-induced shape change causes microtubule instability.
  • To elucidate the role of tubulin conformation in microtubule dynamics.

Main Methods:

  • Utilized coarse-grained molecular dynamics simulations of microtubule models.
  • Incorporated a simulated compression of alpha-subunits, mimicking experimental dephosphorylation effects.
  • Analyzed the impact of this conformational change on microtubule stability and depolymerization.

Main Results:

  • Simulated alpha-subunit compression induced microtubule depolymerization in stable systems.
  • Depolymerization occurred via characteristic microtubule 'ram's horn' unpeeling.
  • GTP-tubulin caps (uncompressed alpha-subunits) effectively prevented depolymerization.

Conclusions:

  • The conformational change of tubulin upon dephosphorylation is sufficient to drive microtubule depolymerization.
  • Microtubule stability is critically dependent on the mechanical state of its subunits.
  • GTP-tubulin rich end caps act as crucial stabilizers against depolymerization.