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Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation

Academic Article
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Overview

authors

  • Truong, T. H.
  • Carroll, Kate

publication date

  • 2012

journal

  • Biochemistry  Journal

abstract

  • Epidermal growth factor receptor (EGFR) exemplifies the family of receptor tyrosine kinases that mediate numerous cellular processes, including growth, proliferation, and differentiation. Moreover, gene amplification and EGFR mutations have been identified in a number of human malignancies, making this receptor an important target for the development of anticancer drugs. In addition to ligand-dependent activation and concomitant tyrosine phosphorylation, EGFR stimulation results in the localized generation of H(2)O(2) by NADPH-dependent oxidases. In turn, H(2)O(2) functions as a secondary messenger to regulate intracellular signaling cascades, largely through the modification of specific cysteine residues within redox-sensitive protein targets, including Cys797 in the EGFR active site. In this review, we highlight recent advances in our understanding of the mechanisms that underlie redox regulation of EGFR signaling and how these discoveries may form the basis for the development of new therapeutic strategies for targeting this and other H(2)O(2)-modulated pathways.

subject areas

  • Cysteine
  • Epidermal Growth Factor
  • Humans
  • Hydrogen Peroxide
  • Membrane Glycoproteins
  • NADPH Oxidase
  • Oxidation-Reduction
  • Phosphorylation
  • Receptor, Epidermal Growth Factor
  • Second Messenger Systems
  • Signal Transduction
  • Sulfenic Acids
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Identity

PubMed Central ID

  • PMC3525721

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi301441e

PubMed ID

  • 23186290
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Additional Document Info

start page

  • 9954

end page

  • 9965

volume

  • 51

issue

  • 50

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