Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction

Corinne M. Spickett, Andrew R. Pitt, Nicolas Morrice, Walter Kolch

Research output: Contribution to journalArticlepeer-review


Signal transduction pathways control cell fate, survival and function. They are organized as intricate biochemical networks which enable biochemical protein activities, crosstalk and subcellular localization to be integrated and tuned to produce highly specific biological responses in a robust and reproducible manner. Post translational Modifications (PTMs) play major roles in regulating these processes through a wide variety of mechanisms that include changes in protein activities, interactions, and subcellular localizations. Determining and analyzing PTMs poses enormous challenges. Recent progress in mass spectrometry (MS) based proteomics have enhanced our capability to map and identify many PTMs. Here we review the current state of proteomic PTM analysis relevant for signal transduction research, focusing on two areas: phosphorylation, which is well established as a widespread key regulator of signal transduction; and oxidative modifications, which from being primarily viewed as protein damage now start to emerge as important regulatory mechanisms.
Original languageEnglish
Pages (from-to)1823-1841
Number of pages19
JournalBBA - Proteins and Proteomics
Issue number12
Publication statusPublished - Dec 2006


  • signal transduction
  • proteomics
  • phosphorylation
  • oxidation
  • nitrosylation
  • post translational modifications
  • Chemistry
  • Biology


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