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Redox regulation of protein kinases

Academic Article
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Overview

authors

  • Truong, T. H.
  • Carroll, Kate

publication date

  • 2013

journal

  • Critical Reviews in Biochemistry and Molecular Biology  Journal

abstract

  • Protein kinases represent one of the largest families of genes found in eukaryotes. Kinases mediate distinct cellular processes ranging from proliferation, differentiation, survival, and apoptosis. Ligand-mediated activation of receptor kinases can lead to the production of endogenous hydrogen peroxide (H₂O₂) by membrane-bound NADPH oxidases. In turn, H₂O₂ can be utilized as a secondary messenger in signal transduction pathways. This review presents an overview of the molecular mechanisms involved in redox regulation of protein kinases and its effects on signaling cascades. In the first half, we will focus primarily on receptor tyrosine kinases (RTKs), whereas the latter will concentrate on downstream non-receptor kinases involved in relaying stimulant response. Select examples from the literature are used to highlight the functional role of H₂O₂ regarding kinase activity, as well as the components involved in H₂O₂ production and regulation during cellular signaling. In addition, studies demonstrating direct modulation of protein kinases by H₂O₂ through cysteine oxidation will be emphasized. Identification of these redox-sensitive residues may help uncover signaling mechanisms conserved within kinase subfamilies. In some cases, these residues can even be exploited as targets for the development of new therapeutics. Continued efforts in this field will further basic understanding of kinase redox regulation, and delineate the mechanisms involved in physiological and pathological H₂O₂ responses.

subject areas

  • Animals
  • Humans
  • Hydrogen Peroxide
  • Oxidation-Reduction
  • Protein Kinases
  • Signal Transduction
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Research

keywords

  • Cysteine
  • NADPH oxidase
  • growth factor signaling
  • hydrogen peroxide
  • protein kinases
  • protein oxidation
  • redox regulation
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Identity

PubMed Central ID

  • PMC4358782

International Standard Serial Number (ISSN)

  • 1040-9238

Digital Object Identifier (DOI)

  • 10.3109/10409238.2013.790873

PubMed ID

  • 23639002
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Additional Document Info

start page

  • 332

end page

  • 356

volume

  • 48

issue

  • 4

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