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Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
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A practical recipe to survey phosphoproteomes.

William C Edelman1, Kelsey M Haas, Joanne I Hsu

  • 1Department of Genome Sciences, University of Washington, Foege S133C, 3720 15th Ave. NE, Seattle, WA, 98105, USA.

Methods in Molecular Biology (Clifton, N.J.)
|May 6, 2014
PubMed
Summary

Discovering new protein phosphorylation events is key to understanding cellular signaling. This study details a robust phosphoproteomics workflow using mass spectrometry for large-scale phosphorylation analysis, from enrichment to data interpretation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • Cellular signaling relies on protein phosphorylation events.
  • Phosphoproteomics enables large-scale identification of protein phosphorylation.
  • Advancements in mass spectrometry have improved phosphoproteomics.

Purpose of the Study:

  • To describe the current state of phosphoproteomics.
  • To present a comprehensive workflow for large-scale phosphorylation analysis.

Main Methods:

  • Phosphopeptide enrichment using Immobilized Metal Affinity Chromatography (IMAC).
  • Mass spectrometry for high-sensitivity, high-resolution analysis.
  • Bioinformatics for data analysis of phosphorylation sites.

Main Results:

  • Established a robust workflow for phosphoproteomics.
  • Facilitated unbiased, discovery-driven identification of phosphosites.
  • Demonstrated improved sensitivity, resolution, and speed in analysis.

Conclusions:

  • Phosphoproteomics is an increasingly accessible field.
  • The presented workflow aids in large-scale phosphorylation analysis.
  • This approach advances the study of cellular signaling pathways.