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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

8.8K

Redox-dependent regulation of epidermal growth factor receptor signaling

David E Heppner1, Albert van der Vliet1

  • 1Department of Pathology and Laboratory Medicine, Vermont Lung Center, University of Vermont, Burlington, VT 05405, United States.

Redox Biology
|January 2, 2016
PubMed

Insights

NADPH oxidases (NOXs) regulate tyrosine phosphorylation, a key cell signaling process in multicellular organisms. This review focuses on NOX-dependent control of the epidermal growth factor receptor (EGFR) pathway.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Signal Transduction

Background:

  • Tyrosine phosphorylation is crucial for cell differentiation and function in multicellular organisms.
  • NADPH oxidases (NOXs) are linked to tyrosine kinase signaling.
  • Redox regulation of tyrosine phosphorylation involves cysteine oxidation in signaling proteins.

Purpose of the Study:

  • To review NOX-dependent regulation of tyrosine kinase signaling pathways.
  • To highlight recent concepts in NOX regulation of the epidermal growth factor receptor (EGFR).

Main Methods:

  • This is a Graphical Redox Review, synthesizing existing research.
  • Focuses on conceptual understanding and pathway regulation.

Main Results:

  • NOX enzymes modulate tyrosine phosphorylation through cysteine oxidation.
  • EGFR signaling is a key example of redox-regulated tyrosine kinase activity.
  • NOX activity impacts EGFR function in normal and pathological conditions.

Conclusions:

  • NOX-dependent redox regulation is a significant mechanism controlling tyrosine kinase signaling.
  • Understanding NOX-EGFR interactions is vital for insights into cancer and oxidative stress pathologies.
Keywords:
Cysteine oxidationEGFRNADPH oxidaseNOX/DUOXTyrosine kinaseTyrosine phosphatase

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