The application of mass spectrometry to membrane proteomics
Christine C. Wu1
& John R. Yates III1, 2
1
Department of Cell Biology, The Scripps Research
Institute, La Jolla, CA 92037
2
Department of Proteomics and Metabolomics, Torrey
Mesa Research Institute, 3115 Merryfield Row, San Diego,
CA 92121-1125.
Correspondence should be addressed to John R. Yates III jyates@scripps.edu
Membrane proteins perform some of the most important functions in
the cell, including the regulation of cell signaling through surface receptors,
cell−cell interactions, and the intracellular compartmentalization of
organelles. Recent developments in proteomic strategies have focused on the
inclusion of membrane proteins in high-throughput analyses. While slow and
steady progress continues to be made in gel-based technologies, significant
advances have been reported in non-gel shotgun methods using liquid
chromatography coupled to mass spectrometry (LC/MS). These latter strategies
facilitate the identification of large numbers of membrane proteins and
modifications, and have the potential to provide insights into protein topology
and orientation in membranes.
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