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Related Concept Videos

Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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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 assembly and...
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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 of...
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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Updated: May 8, 2026

Simultaneous Visualization of the Dynamics of Crosslinked and Single Microtubules In Vitro by TIRF Microscopy
07:20

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Published on: February 18, 2022

Rapid microtubule self-assembly kinetics.

Melissa K Gardner1, Blake D Charlebois, Imre M Jánosi

  • 1Department of Biomedical Engineering, University of Minnesota, Minneapolis, MN 55455, USA.

Cell
|August 23, 2011
PubMed
Summary
This summary is machine-generated.

Microtubule assembly kinetics are faster than previously thought. Increased free subunit concentration enhances both microtubule subunit association and dissociation rates, challenging existing models.

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Simultaneous Visualization of the Dynamics of Crosslinked and Single Microtubules In Vitro by TIRF Microscopy
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Area of Science:

  • Cell Biology
  • Biophysics

Background:

  • Microtubule assembly is crucial for cellular functions.
  • Existing models assume constant subunit dissociation rates, irrespective of free subunit concentration.

Purpose of the Study:

  • To investigate the influence of free subunit concentration on microtubule assembly kinetics.
  • To challenge the assumption of independent dissociation rates in current models.

Main Methods:

  • Utilized Total-Internal-Reflection-Fluorescence (TIRF) microscopy.
  • Employed a laser tweezers assay for high-resolution in vitro microtubule assembly measurements.

Main Results:

  • Demonstrated that microtubule subunit dissociation rate increases with free subunit concentration.
  • Observed a shift in microtubule tip structure from blunt to tapered with increasing concentration.
  • Found that both association and dissociation rates increase at higher concentrations.

Conclusions:

  • Microtubule assembly kinetics are significantly faster, by an order of magnitude, than previously estimated.
  • The findings support a two-dimensional model of microtubule assembly influenced by tip structure.
  • Revises fundamental understanding of microtubule dynamics and regulation.