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Cadmium-induced proteome remodeling regulated by Spc1/Sty1 and Zip1 in fission yeast

Academic Article
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Overview

authors

  • Guo, L.
  • Ghassemian, M.
  • Komives, E. A.
  • Russell, Paul

publication date

  • 2012

journal

  • Toxicological Sciences  Journal

abstract

  • Stress-activated protein kinases and transcription factors are crucial for surviving exposure to cadmium and other environmental toxicants, but their effects on the proteome remain largely unexplored. In this study, isobaric tag for relative and absolute quantitation reveals that cadmium stress triggers rapid proteome remodeling in the fission yeast Schizosaccharomyces pombe. Spc1/Sty1, a mitogen/stress-activated protein kinase homologous to human p38 and Saccharomyces cerevisiae Hog1, controls many of these changes, including enzymes of the oxidative phase of the pentose phosphate pathway and trehalose metabolism. Genetic studies indicate that control of carbohydrate metabolism by Spc1 is required for cadmium tolerance. The bZIP transcription factor Zip1, which is functionally related to human Nrf2 and S. cerevisiae Met4, has a smaller effect on cadmium-induced proteome remodeling, but it is required for production of key proteins involved in sulfur metabolism, which are essential for cadmium resistance. These studies reveal how Spc1 and Zip1 independently reshape the proteome to modulate cellular defense mechanisms against the toxic effects of cadmium.

subject areas

  • Cadmium
  • Mitogen-Activated Protein Kinases
  • Proteome
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Transcriptome
  • Trehalose
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Research

keywords

  • MAPK
  • Schizosaccharomyces pombe
  • cadmium
  • heavy metals
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Identity

PubMed Central ID

  • PMC3713068

International Standard Serial Number (ISSN)

  • 1096-6080

Digital Object Identifier (DOI)

  • 10.1093/toxsci/kfs179

PubMed ID

  • 22610605
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Additional Document Info

start page

  • 200

end page

  • 212

volume

  • 129

issue

  • 1

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