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Originally published In Press as doi:10.1074/mcp.M300079-MCP200 on September 29, 2003.
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Molecular & Cellular Proteomics 2:1261-1270, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Proteomic Analysis of Glycosylphosphatidylinositol-anchored Membrane Proteins*

Felix Elortza{ddagger},§, Thomas S. Nühse,||, Leonard J. Foster{ddagger},**, Allan Stensballe{ddagger}, Scott C. Peck and Ole N. Jensen{ddagger},{ddagger}{ddagger}

From the {ddagger} Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark and Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, United Kingdom

Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are a functionally and structurally diverse family of post-translationally modified membrane proteins found mostly in the outer leaflet of the plasma membrane in a variety of eukaryotic cells. Although the general role of GPI-APs remains unclear, they have attracted attention because they act as enzymes and receptors in cell adhesion, differentiation, and host-pathogen interactions. GPI-APs may represent potential diagnostic and therapeutic targets in humans and are interesting in plant biotechnology because of their key role in root development. We here present a general mass spectrometry-based proteomic "shave-and-conquer" strategy that specifically targets GPI-APs. Using a combination of biochemical methods, mass spectrometry, and computational sequence analysis we identified six GPI-APs in a Homo sapiens lipid raft-enriched fraction and 44 GPI-APs in an Arabidopsis thaliana membrane preparation, representing the largest experimental dataset of GPI-anchored proteins to date.

{ddagger}{ddagger} To whom correspondence should be addressed. Tel.: 45-6550-2368; Fax: 45-6550-2467; E-mail: jenseno{at}bmb.sdu.dk


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