Tools for phospho- and glycoproteomics of plasma membranes

Amino Acids. 2011 Jul;41(2):223-33. doi: 10.1007/s00726-010-0796-8.


Analysis of plasma membrane proteins and their posttranslational modifications is considered as important for identification of disease markers and targets for drug treatment. Due to their insolubility in water, studying of plasma membrane proteins using mass spectrometry has been difficult for a long time. Recent technological developments in sample preparation together with important improvements in mass spectrometric analysis have facilitated analysis of these proteins and their posttranslational modifications. Now, large scale proteomic analyses allow identification of thousands of membrane proteins from minute amounts of sample. Optimized protocols for affinity enrichment of phosphorylated and glycosylated peptides have set new dimensions in the depth of characterization of these posttranslational modifications of plasma membrane proteins. Here, I summarize recent advances in proteomic technology for the characterization of the cell surface proteins and their modifications. In the focus are approaches allowing large scale mapping rather than analytical methods suitable for studying individual proteins or non-complex mixtures.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biotinylation / methods
  • Cell Fractionation / methods
  • Cell Membrane / chemistry*
  • Cell Membrane / metabolism
  • Chromatography, Liquid / methods
  • Humans
  • Membrane Glycoproteins / chemistry*
  • Membrane Glycoproteins / metabolism
  • Peptide Fragments / chemistry
  • Peptide Mapping / methods
  • Phosphoproteins / chemistry*
  • Phosphoproteins / metabolism
  • Protein Processing, Post-Translational
  • Proteomics / methods*
  • Tandem Mass Spectrometry / methods


  • Membrane Glycoproteins
  • Peptide Fragments
  • Phosphoproteins