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Related Experiment Videos

Vimentin's tail interacts with actin-containing structures in vivo

R B Cary1, M W Klymkowsky, R M Evans

  • 1University of Colorado, Boulder 80309-0347.

Journal of Cell Science
|June 1, 1994
PubMed
Summary

The vimentin tail domain interacts with actin structures in cells, suggesting a role in organizing intermediate filaments and microfilaments. This interaction is specific and not due to simple charge association.

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Area of Science:

  • Cell Biology
  • Cytoskeletal Dynamics
  • Protein Interactions

Background:

  • Intermediate filaments (IFs) are crucial cytoskeletal components.
  • The tail domain of vimentin is known to be dispensable for IF assembly in vitro.

Purpose of the Study:

  • To investigate the in vivo function of the vimentin tail domain.
  • To determine if the vimentin tail domain interacts with other cytoskeletal elements.

Main Methods:

  • Constructed and purified a myc-tagged Xenopus vimentin-1 tail domain (mycVimTail).
  • Injected mycVimTail into cultured Xenopus A6 cells and observed co-localization with actin.
  • Used control myc-tagged polypeptides (lamin tail, similar charge/mass polypeptide) to assess specificity.

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Main Results:

  • mycVimTail co-localized with actin-containing structures in cells.
  • Control polypeptides showed nuclear localization (lamin) or no association with actin, confirming specificity.
  • myc-tagged keratin DG81A tail polypeptides were insoluble and aggregated, indicating different physical properties compared to vimentin tail.

Conclusions:

  • Vimentin's tail domain possesses a highly extended structure.
  • The vimentin tail domain binds to actin-containing structures.
  • This interaction may mediate cross-talk between vimentin filaments and microfilaments, influencing vimentin filament organization.