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Updated: Aug 9, 2026

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
09:16

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy

Published on: September 11, 2015

Conformational analysis of the phosphorylated epidermal growth factor receptor

A Bishayee1, L Beguinot, S Bishayee

  • 1Department of Pathology and Laboratory Medicine, UMDNJ-New Jersey Medical School, Newark 07103-2714, USA.

Bioscience Reports
|April 14, 2000
PubMed

Insights

This study identifies specific domains and phosphate-accepting tyrosine residues in the epidermal growth factor receptor (EGFR) responsible for phosphorylation-induced conformational changes, advancing our understanding of receptor signaling.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Conformational changes in receptor tyrosine kinases upon phosphorylation are known.
  • Specific epitopes and tyrosine residues driving these alterations remain largely unidentified.

Purpose of the Study:

  • To pinpoint the specific domain within the C-terminal tail of the epidermal growth factor receptor (EGFR) involved in conformational changes.
  • To identify the precise tyrosine residue(s) acting as phosphate acceptors in this process.

Main Methods:

  • Utilized a conformation-specific anti-peptide antibody.
  • Investigated structural alterations in the EGFR C-terminal tail.

Main Results:

  • Successfully identified a specific domain in the EGFR C-terminal tail.
  • Pinpointed the tyrosine residue(s) responsible for mediating phosphorylation-induced conformational changes.

Conclusions:

  • The study elucidates key structural elements and phosphorylation sites in EGFR.
  • Provides a foundation for understanding EGFR signaling and potential therapeutic targeting.

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