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Related Experiment Videos

A novel interaction between kinesin and p120 modulates p120 localization and function.

Masahiro Yanagisawa1, Irina N Kaverina, Aixia Wang

  • 1Mayo Clinic Cancer Center, Jacksonville, Florida 32224, USA.

The Journal of Biological Chemistry
|December 17, 2003
PubMed
Summary

Cytoplasmic p120-catenin directly and indirectly binds microtubules via kinesin, influencing its cellular localization and activity. This interaction impacts p120

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cytoskeletal Dynamics

Background:

  • p120-catenin (also known as p120) has known roles in cadherin regulation and transcriptional repression via Kaiso.
  • Its localization includes membrane-associated, cytosolic, and nuclear pools.

Purpose of the Study:

  • To investigate the association of p120-catenin with the microtubule network.
  • To elucidate the mechanisms and functional consequences of p120-catenin's interaction with microtubules and kinesin.

Main Methods:

  • Co-immunoprecipitation assays to detect protein interactions.
  • Microtubule perturbation using nocodazole and taxol.
  • Overexpression of p120-catenin and kinesin fragments.
  • Confocal microscopy to assess protein localization.

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Main Results:

  • Cytoplasmic p120-catenin directly binds to microtubules via its armadillo repeats, an interaction mutually exclusive with E-cadherin binding.
  • p120-catenin indirectly binds microtubules through conventional kinesin heavy chains.
  • Disrupting microtubule interactions alters the cytoplasmic-nuclear balance of p120-catenin.
  • Kinesin-mediated transport influences p120-catenin localization and activity, affecting cellular phenotypes.

Conclusions:

  • p120-catenin interacts with the microtubule cytoskeleton through both direct and kinesin-dependent mechanisms.
  • Kinesin plays a crucial role in regulating p120-catenin's subcellular targeting and function.
  • These findings reveal a novel regulatory pathway for p120-catenin localization and activity.