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Disassembly of Intermediate Filaments01:35

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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
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Related Experiment Video

Updated: Jan 20, 2026

Disassembly of Intermediate Filaments
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Structural Dynamics of Nonenveloped Virus Disassembly Intermediates.

Kimi Azad1, Manidipa Banerjee2

  • 1Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, New Delhi, India.

Journal of Virology
|September 6, 2019
PubMed
Summary

Icosahedral virus disassembly is key for infection. Researchers used incremental heating to find that genome release is a localized, asymmetric process, not a global one, revealing new insights into viral uncoating.

Keywords:
Flock House virusasymmetric reconstructioncryo-electron microscopydisassemblysingle-particle 3D analysis

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Area of Science:

  • Structural biology
  • Virology
  • Biochemistry

Background:

  • Icosahedral virus stability is essential for genome protection during transit.
  • Viral infection requires capsid disassembly, but the process and intermediates are poorly understood.

Purpose of the Study:

  • To characterize the disassembly pathway of a model nonenveloped virus.
  • To identify and structurally analyze transient intermediates during capsid disassembly.

Main Methods:

  • Incremental heating to induce and isolate disassembly intermediates.
  • Cryo-electron microscopy and 3D reconstruction to determine intermediate structures without symmetry constraints.

Main Results:

  • Two distinct disassembly intermediates, "eluted particles" and "puffed particles," were identified.
  • Structural analysis revealed asymmetric alterations in the capsid during disassembly.
  • Genome release was localized to a specific region on the capsid, occurring through the 2-fold axis.

Conclusions:

  • Virus disassembly is a programmed, asymmetric conformational change.
  • The process involves localized structural alterations rather than global capsid destabilization.
  • Understanding these mechanisms provides insights into viral infection and capsid dynamics.