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Submitted on August 19, 2003
Biochemistry & Molecular Biology, University of Southern Denmark, Odense DK-5230
Corresponding Author: jenseno{at}bmb.sdu.dk
Glycosyl-phosphatidylinositol 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 H. sapiens lipid raft-enriched fraction and 44 GPI-APs in a A. thaliana membrane preparation, representing the largest experimental data set of GPI anchored proteins to date.
Revised on September 24, 2003
Accepted on September 29, 2003
Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins
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