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Related Experiment Videos

Assessing the flexibility of intermediate filaments by atomic force microscopy.

N Mücke1, L Kreplak, R Kirmse

  • 1Division Biophysics of Macromolecules, German Cancer Research Center, 69120 Heidelberg, Germany. norbert.muecke@dkfz-heidelberg.de

Journal of Molecular Biology
|January 20, 2004
PubMed
Summary

This study quantifies the flexibility of intermediate filaments (IFs), revealing their persistence length in solution is approximately 1 micrometer. This flexibility stems from linker regions and dimer slipping within IFs, contrasting with stiffer actin and microtubule cytoskeletal structures.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Cytoskeletal Dynamics

Background:

  • Eukaryotic cells possess three distinct cytoskeletal filament systems: microtubules, microfilaments, and intermediate filaments (IFs).
  • Microtubules and microfilaments are stiff, polar structures influenced by nucleotide hydrolysis.
  • Intermediate filaments are flexible, apolar structures built from coiled-coil dimers, but their quantitative mechanical properties remain largely uncharacterized.

Purpose of the Study:

  • To quantitatively determine the persistence length of intermediate filaments (IFs).
  • To compare the flexibility of IFs with other cytoskeletal elements like actin and microtubules.
  • To elucidate the structural basis for IF flexibility.

Main Methods:

  • Atomic Force Microscopy (AFM) was used to image individual vimentin IFs in physiological buffer.

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  • Transmission Electron Microscopy (TEM) of negatively stained dehydrated filaments was employed for comparison.
  • Persistence length was measured for IFs adsorbed to various solid supports.

    • Main Results:

    • Apparent persistence length of adsorbed IFs ranged from 0.3 to 1 micrometer.
    • Estimated persistence length of IFs in dilute solution is approximately 1 micrometer.
    • IFs exhibit lower persistence length compared to F-actin filaments and microtubules.

    Conclusions:

    • Intermediate filaments are significantly more flexible than previously assumed, with a persistence length comparable to F-actin.
    • The flexibility of IFs is attributed to flexible linker regions within their coiled-coil dimers and potential axial slipping between dimers.
    • These findings provide crucial quantitative data on IF mechanical properties and their contribution to cellular mechanics.