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Related Experiment Videos

Assembly of intermediate filaments

R L Shoeman1, P Traub

  • 1Max-Planck-Institut für Zellbiologie, Ladenburg, Federal Republic of Germany.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|September 1, 1993
PubMed
Summary

Intermediate filament assembly is driven by the central rod domain

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Area of Science:

  • Cell biology
  • Biochemistry
  • Structural biology

Background:

  • Intermediate filaments are a fundamental class of cytoskeletal proteins.
  • Their central rod domain, rich in alpha-helices, dictates assembly.
  • Assembly can occur in vitro without external energy sources.

Purpose of the Study:

  • To elucidate the self-assembly mechanism of intermediate filaments.
  • To identify the key protein domains and interactions involved in filament formation.
  • To understand the role of end domains and rod termini in modulating assembly.

Main Methods:

  • In vitro assembly assays.
  • Analysis of protein-protein interactions (coiled-coil, lateral, longitudinal).
  • Investigation of the role of non-alpha-helical end domains and rod termini.

Main Results:

  • Intermediate filament assembly initiates with parallel, in-register dimers formed by coiled-coil interactions.
  • Dimers further associate into tetramers through staggered arrangements (parallel or antiparallel).
  • Increased ionic strength promotes spontaneous polymerization of dimers and tetramers into 10 nm filaments via poorly understood intermediates.

Conclusions:

  • The central rod domain's alpha-helical coiled-coil interactions are crucial for dimer and tetramer formation.
  • Non-alpha-helical end domains and specific rod termini residues modulate higher-order filament assembly.
  • The same interactions governing tetramer formation likely drive lateral and longitudinal associations in mature intermediate filaments.

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