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Related Experiment Videos

Surface distribution and internalization of erbB-2 proteins.

L V Lotti1, C Di Lazzaro, C Zompetta

  • 1Istituto Nazionale Ricerca sul Cancro di Genova, Sezione di Biotecnologie, Rome, Italy.

Experimental Cell Research
|October 1, 1992
PubMed
Summary

The erbB-2 proto-oncogene product (p185) is internalized similarly to the epidermal growth factor receptor (EGFR) upon antibody binding. Mutations in erbB-2 can lead to its constitutive internalization.

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Area of Science:

  • Cell biology
  • Molecular oncology
  • Protein trafficking

Background:

  • The erbB-2 proto-oncogene product (p185) is structurally related to the epidermal growth factor receptor (EGFR).
  • Understanding the cell surface localization and internalization pathways of p185 is crucial for cancer research.

Purpose of the Study:

  • To investigate the cell surface localization and early internalization steps of erbB-2/p185.
  • To compare the internalization pathway of erbB-2/p185 with that of EGFR.
  • To determine the effect of mutations on erbB-2 internalization.

Main Methods:

  • Immunofluorescence microscopy to track protein localization.
  • Antibody-induced internalization assays at 37°C.
  • Analysis of wild-type and mutant erbB-2 proteins, including a chimeric EGFR/erbB-2 molecule.

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Main Results:

  • erbB-2/p185 is primarily excluded from cell surface endocytic pits.
  • Anti-erbB-2 antibody triggers rapid internalization of p185.
  • A chimeric EGFR/erbB-2 molecule shows EGF-induced internalization.
  • Internalization timing and pathways for erbB-2/p185 resemble those of EGFR.
  • Mutant activated erbB-2 proteins are often found in endocytic pits.

Conclusions:

  • The internalization of erbB-2/p185 is similar to EGFR, suggesting conserved mechanisms.
  • Mutations within the transmembrane regions of erbB-2 can induce constitutive internalization.
  • These findings have implications for understanding erbB-2-driven oncogenesis and potential therapeutic strategies.