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Related Experiment Videos

Association with membrane protrusions makes ErbB2 an internalization-resistant receptor.

Anette M Hommelgaard1, Mads Lerdrup, Bo van Deurs

  • 1Structural Cell Biology Unit, Department of Medical Anatomy, The Panum Institute, University of Copenhagen, Copenhagen 2200 N, Denmark.

Molecular Biology of the Cell
|January 27, 2004
PubMed
Summary

ErbB2 receptors resist internalization by associating with membrane protrusions, avoiding clathrin-coated pits. This resistance, unlike other growth factor receptors, is key to ErbB2

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • ErbB2, unlike the epidermal growth factor (EGF) receptor, persists at the plasma membrane post-ligand binding and dimerization.
  • The mechanism behind ErbB2's lack of efficient down-regulation remains unclear, with possibilities including internalization resistance or efficient recycling.

Purpose of the Study:

  • To investigate the reasons for ErbB2's resistance to down-regulation.
  • To elucidate the cellular mechanisms governing ErbB2 localization and internalization.

Main Methods:

  • Confocal microscopy
  • Immunogold labeling electron microscopy
  • Biochemical techniques

Main Results:

Related Experiment Videos

  • ErbB2 is preferentially localized to membrane protrusions and excluded from clathrin-coated pits.
  • ErbB2 is not found in transferrin receptor-containing endosomes, irrespective of ligand (EGF, heregulin) or antibody (herceptin) binding.
  • Exclusion from coated pits is pronounced and not solely due to a lack of internalization signals.
  • ErbB2 localization to protrusions is independent of raft association and actin cytoskeleton integrity.
  • Cross-linking ErbB2 leads to its redistribution to bulk membrane, coated pits, and endosomes.

    • Conclusions:

    • ErbB2 is a highly internalization-resistant receptor.
    • The firm association of ErbB2 with membrane protrusions is the likely reason for its internalization resistance.